Job Results:

Ligand

Structure

Job ID

88f5e34b49c349e8fb2dad2534e9dc3f

Job name

Davis_Task36

Time

2024-08-15 20:29:54

Rank Target PDB ID AirScore Detail
1Endothelin-converting enzyme 1 (ECE1)3DWB8.92
Target general information
Gen name
ECE1
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
ECE-1
Protein family
Peptidase M13 family
Biochemical class
Peptidase
Function
Converts big endothelin-1 to endothelin-1.
Related diseases
Hirschsprung disease, cardiac defects, and autonomic dysfunction (HCAD) [MIM:613870]: A disorder characterized by skip-lesions Hirschsprung disease, craniofacial abnormalities and other dysmorphic features, cardiac defects including ductus arteriosus, small subaortic ventricular septal defect, small atrial septal defect, and autonomic dysfunction. {ECO:0000269|PubMed:9915973}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07171
Interacts with
P49760; A8MQ03; Q8IUG1; P60370; P60410
EC number
EC 3.4.24.71
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Disease variant; Disulfide bond; Glycoprotein; Hirschsprung disease; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteomics identification; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; Zinc
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

75247.9
Length
660
Aromaticity
0.12
Instability index
46.29
Isoelectric point
5.33
Charge

(pH=7)

-18.3
2D Binding mode
Binding energy

(Kcal/mol)

-8.24
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW
Hydrogen bonds contact
Hydrophobic contact
2Coagulation factor Xa (F10)2JKH8.56
Target general information
Gen name
F10
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Fxa; Factor Xa; F10; Activated coagulation factor X
Protein family
Peptidase S1 family
Biochemical class
Peptidase
Function
Factor Xa is avitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Related diseases
Factor X deficiency (FA10D) [MIM:227600]: A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis. {ECO:0000269|PubMed:10468877, ECO:0000269|PubMed:10739379, ECO:0000269|PubMed:10746568, ECO:0000269|PubMed:11248282, ECO:0000269|PubMed:11728527, ECO:0000269|PubMed:12574802, ECO:0000269|PubMed:12945883, ECO:0000269|PubMed:15075089, ECO:0000269|PubMed:15650540, ECO:0000269|PubMed:17393015, ECO:0000269|PubMed:19135706, ECO:0000269|PubMed:1973167, ECO:0000269|PubMed:1985698, ECO:0000269|PubMed:25313940, ECO:0000269|PubMed:26222694, ECO:0000269|PubMed:2790181, ECO:0000269|PubMed:7669671, ECO:0000269|PubMed:7860069, ECO:0000269|PubMed:8529633, ECO:0000269|PubMed:8845463, ECO:0000269|PubMed:8910490}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07211; DB08746; DB07974; DB07277; DB07605; DB08487; DB08495; DB04673; DB08745; DB08488; DB07804; DB08174; DB08173; DB07872; DB07843; DB07848; DB07875; DB08143; DB07847; DB07844; DB13884; DB06552; DB13151; DB13192; DB00025; DB11166; DB06605; DB09258; DB12364; DB00100; DB13152; DB13150; DB00036; DB09075; DB16662; DB13923; DB01225; DB06920; DB00569; DB03847; DB07278; DB01109; DB06406; DB09332; DB06245; DB13998; DB05713; DB13999; DB07630; DB07629; DB07973; DB07800; DB12598; DB13933; DB06635; DB09141; DB13149; DB11311; DB06228; DB05362; DB07261; DB08426; DB09109; DB14738
Interacts with
P0DPK4; Q9UK55; Q9UHD9
EC number
EC 3.4.21.6
Uniprot keywords
3D-structure; Blood coagulation; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Disease variant; Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; Hydroxylation; Protease; Proteomics identification; Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

31315.2
Length
280
Aromaticity
0.09
Instability index
38.33
Isoelectric point
6.36
Charge

(pH=7)

-1.82
2D Binding mode
Binding energy

(Kcal/mol)

-9.01
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLERDWAESMTQKTGIVSGFGRTHEKGEQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARGKYGIYTKVTAFLKWIDRSMKKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERR
Hydrogen bonds contact
Hydrophobic contact
3Cytochrome P450 1A22HI48.52
Target general information
Gen name
CYP1A2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
Cytochrome P450 family
Biochemical class
Oxidoreductase
Function
Aromatase activity.Caffeine oxidase activity.Demethylase activity.Electron carrier activity.Enzyme binding.Heme binding.Iron ion binding.Monooxygenase activity.Oxidoreductase activity.Oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen.Oxygen binding.
Related diseases
Myeloperoxidase deficiency (MPOD) [MIM:254600]: A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis. {ECO:0000269|PubMed:37198333, ECO:0000269|PubMed:7904599, ECO:0000269|PubMed:8142659, ECO:0000269|PubMed:8621627, ECO:0000269|PubMed:9354683, ECO:0000269|PubMed:9637725}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB08496; DB01667; DB14132; DB04356; DB02489; DB11932; DB12001; DB05812; DB13573; DB01418; DB00316; DB15568; DB06594; DB00518; DB05396; DB00969; DB07453; DB01424; DB01223; DB01118; DB00321; DB00261; DB01217; DB01435; DB06605; DB05676; DB06413; DB06216; DB01072; DB15011; DB06442; DB06626; DB00993; DB00972; DB13203; DB05015; DB16703; DB06769; DB01086; DB06770; DB06771; DB06732; DB00195; DB04889; DB11967; DB13975; DB00188; DB12151; DB01558; DB14018; DB13812; DB00201; DB09061; DB14737; DB11791; DB06774; DB00564; DB06016; DB01136; DB12814; DB00477; DB00356; DB01166; DB00501; DB01012; DB00568; DB00827; DB00537; DB00215; DB12499; DB14025; DB00349; DB01242; DB00575; DB00758; DB00363; DB00286; DB11672; DB14635; DB00924; DB08912; DB00851; DB06292; DB01254; DB01609; DB01151; DB16650; DB12161; DB01191; DB00633; DB11994; DB00586; DB11511; DB12945; DB00280; DB01184; DB09167; DB05928; DB01142; DB09273; DB00470; DB00476; DB00625; DB15444; DB06210; DB13874; DB11718; DB00467; DB11404; DB00530; DB00783; DB13952; DB13953; DB13954; DB13955; DB13956; DB00655; DB04574; DB13592; DB00330; DB00898; DB00977; DB00773; DB01628; DB00927; DB04854; DB01482; DB00574; DB12265; DB15669; DB01195; DB08972; DB04841; DB00544; DB00472; DB00499; DB00176; DB01320; DB00998; DB14029; DB06160; DB01044; DB01241; DB01155; DB01645; DB01381; DB00986; DB00365; DB00400; DB05708; DB00629; DB00502; DB01094; DB14999; DB04076; DB11737; DB00619; DB00458; DB11564; DB01306; DB09456; DB09564; DB01307; DB00047; DB01309; DB00030; DB00046; DB11567; DB00071; DB11568; DB05258; DB00034; DB00105; DB15131; DB00011; DB00018; DB00069; DB00060; DB00068; DB00033; DB00951; DB11757; DB09570; DB01026; DB01097; DB16217; DB09078; DB01002; DB05667; DB00281; DB12406; DB09198; DB04948; DB00978; DB06448; DB16220; DB01601; DB00455; DB04871; DB06077; DB01283; DB00772; DB00934; DB06234; DB14009; DB00784; DB01065; DB00170; DB00454; DB00532; DB00333; DB00763; DB00553; DB01028; DB09241; DB01233; DB00379; DB06148; DB01388; DB06595; DB00370; DB16236; DB00745; DB11763; DB00218; DB06510; DB14011; DB00461; DB00607; DB00779; DB00788; DB06600; DB00238; DB06803; DB00184; DB01115; DB11793; DB00435; DB05115; DB00717; DB01059; DB00540; DB05990; DB01165; DB00334; DB16267; DB00338; DB00904; DB11632; DB11443; DB01173; DB11837; DB09330; DB01303; DB11697; DB00377; DB00715; DB06589; DB11774; DB00487; DB00008; DB00022; DB09122; DB13634; DB00806; DB11198; DB08883; DB00850; DB03783; DB01174; DB00388; DB00252; DB11450; DB01100; DB13823; DB04951; DB17472; DB11642; DB08910; DB15822; DB01058; DB01087; DB00794; DB00420; DB09288; DB01182; DB06479; DB00818; DB00571; DB13449; DB11892; DB04216; DB00908; DB00468; DB01129; DB00980; DB09290; DB00863; DB01367; DB00409; DB02709; DB13174; DB01045; DB11753; DB00740; DB14924; DB00503; DB00533; DB01656; DB15119; DB00268; DB00296; DB00412; DB00817; DB12332; DB13772; DB06654; DB11491; DB00418; DB01037; DB11689; DB06290; DB13261; DB15093; DB00052; DB00398; DB01208; DB09118; DB00428; DB06820; DB00382; DB00675; DB06083; DB09071; DB05488; DB09256; DB01079; DB01405; DB00857; DB08880; DB11712; DB01412; DB00277; DB00730; DB01623; DB00208; DB06137; DB00697; DB01056; DB06264; DB00752; DB00384; DB12245; DB00831; DB15442; DB00440; DB00685; DB08867; DB14989; DB13609; DB06235; DB00313; DB08881; DB00661; DB09185; DB12026; DB00682; DB02134; DB00549; DB00744; DB00315; DB00425; DB09225; DB09120
Interacts with
O95870
EC number
1.14.14.1; 4.2.1.152
Uniprot keywords
3D-structure; Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid metabolism; Lyase; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Proteomics identification; Reference proteome; Steroid metabolism; Sterol metabolism
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

54475
Length
480
Aromaticity
0.1
Instability index
40.43
Isoelectric point
9.16
Charge

(pH=7)

9.89
2D Binding mode
Binding energy

(Kcal/mol)

-9.64
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
RVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARRFS
Hydrogen bonds contact
Hydrophobic contact
4Human immunodeficiency virus Protease (HIV PR)3TL98.47
Target general information
Gen name
HIV PR
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1)
Uniprot ID
TTD ID
Synonyms
HIV Retropepsin; HIV PR
Protein family
NA
Biochemical class
Peptidase
Function
Gag-Pol polyprotein: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation.
Related diseases
Sitosterolemia 2 (STSL2) [MIM:618666]: A form of sitosterolemia, an autosomal recessive metabolic disorder characterized by unregulated intestinal absorption of cholesterol, phytosterols and shellfish sterols, and decreased biliary excretion of dietary sterols into bile. Patients have hypercholesterolemia, very high levels of plant sterols in the plasma, and frequently develop tendon and tuberous xanthomas, accelerated atherosclerosis and premature coronary artery disease. {ECO:0000269|PubMed:11138003, ECO:0000269|PubMed:11452359, ECO:0000269|PubMed:11668628, ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:35557526}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07035; DB02704; DB07806; DB02785; DB01824; DB01732; DB06874; DB08034; DB07961; DB07451; DB08212; DB08372; DB02972; DB04190; DB04042; DB08428; DB03076; DB03141; DB08457; DB07343; DB07337; DB07018; DB07332; DB05398; DB07578; DB08639; DB06414; DB04255; DB04547; DB02683; DB02009; DB03908; DB02629; DB01887; DB03803; DB02033; DB08281; DB08282; DB08284; DB08414; DB08598; DB07327; DB07885; DB02768; DB08600; DB01891; DB05871
Interacts with
NA
EC number
EC 3.4.23.16
Uniprot keywords
3D-structure; Activation of host caspases by virus; AIDS; Aspartyl protease; Capsid protein; Direct protein sequencing; DNA integration; DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease; Eukaryotic host gene expression shutoff by virus; Eukaryotic host translation shutoff by virus; Host cell membrane; Host cytoplasm; Host endosome; Host gene expression shutoff by virus; Host membrane; Host nucleus; Host-virus interaction; Hydrolase; Lipid-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation; Modulation of host cell apoptosis by virus; Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease; Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase; Transferase; Viral genome integration; Viral nucleoprotein; Viral penetration into host nucleus; Viral release from host cell; Virion; Virion maturation; Virus entry into host cell; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

21934.7
Length
202
Aromaticity
0.06
Instability index
48.65
Isoelectric point
9.66
Charge

(pH=7)

6.15
2D Binding mode
Binding energy

(Kcal/mol)

-8.25
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PQITLWKRPLVTIKIGGQLKEALLDTGADDTVIEEMSLPGRWKPKMIGGIGGFIKVRQYDQIIIEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNFSFNFPQITLWKRPLVTIKIGGQLKEALLDTGADDTVIEEMSLPGRWKPKMIGGIGGFIKVRQYDQIIIEIAGHKAIGTVLVGPTPVNIIGRNLLTQIGATLNF
Hydrogen bonds contact
Hydrophobic contact
5Opioid receptor delta (OPRD1)4N6H8.44
Target general information
Gen name
OPRD1
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
OPRD; Delta-type opioid receptor; Delta opioid receptor; DOR-1; D-OR-1
Protein family
G-protein coupled receptor 1 family
Biochemical class
GPCR rhodopsin
Function
Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine. G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids.
Related diseases
Defects in PPARG can lead to type 2 insulin-resistant diabetes and hyptertension. PPARG mutations may be associated with colon cancer. {ECO:0000269|PubMed:10394368}.; DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by an increase of body weight beyond the limitation of skeletal and physical requirements, as the result of excessive accumulation of body fat. {ECO:0000269|PubMed:9753710}. Disease susceptibility may be associated with variants affecting the gene represented in this entry.; DISEASE: Lipodystrophy, familial partial, 3 (FPLD3) [MIM:604367]: A form of lipodystrophy characterized by marked loss of subcutaneous fat from the extremities. Facial adipose tissue may be increased, decreased or normal. Affected individuals show an increased preponderance of insulin resistance, diabetes mellitus and dyslipidemia. {ECO:0000269|PubMed:11788685, ECO:0000269|PubMed:12453919}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glioma 1 (GLM1) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes. {ECO:0000269|PubMed:10851250}. Disease susceptibility may be associated with variants affecting the gene represented in this entry. Polymorphic PPARG alleles have been found to be significantly over-represented among a cohort of American patients with sporadic glioblastoma multiforme suggesting a possible contribution to disease susceptibility.
Drugs

(DrugBank ID)

DB01571; DB01439; DB05050; DB06274; DB06288; DB00321; DB01238; DB00921; DB00611; DB09173; DB09061; DB01535; DB00318; DB00514; DB00647; DB01452; DB01565; DB01444; DB01081; DB01548; DB09272; DB01497; DB00813; DB00956; DB00327; DB01221; DB06738; DB00854; DB00836; DB14146; DB14009; DB12668; DB00333; DB00295; DB06409; DB14011; DB00844; DB11691; DB06230; DB01183; DB00704; DB11130; DB00497; DB01192; DB09209; DB00899; DB12543; DB00708; DB06204; DB00193
Interacts with
P16615; P27824; Q4LDR2; Q5JY77; Q9NS64; Q9Y666-2; Q9UKG4; Q0VAQ4; Q96Q45-2; P11607
EC number
NA
Uniprot keywords
3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate; Proteomics identification; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix; Ubl conjugation
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

32859.3
Length
294
Aromaticity
0.11
Instability index
33.86
Isoelectric point
9.38
Charge

(pH=7)

13.6
2D Binding mode
Binding energy

(Kcal/mol)

-8.84
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRKPCG
Hydrogen bonds contact
Hydrophobic contact
6Suppressor of tumorigenicity 14 protein (ST14)3P8G8.41
Target general information
Gen name
ST14
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Tumor-associated differentially-expressed gene 15 protein; Tumor associated differentially-expressed gene-15 protein; TADG15; Serine protease TADG-15; Serine protease 14; SNC19; Prostamin; PRSS14; Mem
Protein family
Peptidase S1 family
Biochemical class
Peptidase
Function
Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing. Degrades extracellular matrix.
Related diseases
Ichthyosis, congenital, autosomal recessive 11 (ARCI11) [MIM:602400]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:17273967, ECO:0000269|PubMed:18843291}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB03127; DB13729; DB00013
Interacts with
NA
EC number
EC 3.4.21.109
Uniprot keywords
3D-structure; Disease variant; Disulfide bond; Glycoprotein; Hydrolase; Hypotrichosis; Ichthyosis; Membrane; Protease; Proteomics identification; Reference proteome; Repeat; Serine protease; Signal-anchor; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

26451.5
Length
241
Aromaticity
0.1
Instability index
30.45
Isoelectric point
5.6
Charge

(pH=7)

-5.69
2D Binding mode
Binding energy

(Kcal/mol)

-8.34
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
VVGGTDADEGEWPWQVSLHALGQGHICGASLISPNWLVSAAHCYIDDRGFRYSDPTQWTAFLGLHDQSQRSAPGVQERRLKRIISHPFFNDFTFDYDIALLELEKPAEYSSMVRPICLPDASHVFPAGKAIWVTGWGHTQYGGTGALILQKGEIRVIQQTTCENLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEADGRIFQAGVVSWGDGCAQRNKPGVYTRLPLFRDWIKENTGV
Hydrogen bonds contact
Hydrophobic contact
7Short transient receptor potential channel 5 (TRPC5)7WDB8.39
Target general information
Gen name
TRPC5
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
hTRP5; hTRP-5; TrpC5; Transient receptor protein 5; TRP-5
Protein family
Transient receptor (TC 1.A.4) family, STrpC subfamily, TRPC5 sub-subfamily
Biochemical class
Transient receptor potential catioin channel
Function
Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion.
Related diseases
Loss-of-function variants in TRPC5 may be involved in a mental disorder characterized by maladaptive behavior, anxiety, autism, postpartum depression, extreme food-seeking and hoarding behavior, hyperphagia and obesity. {ECO:0000269|PubMed:38959890}.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane; Disease variant; Glycoprotein; Ion channel; Ion transport; Membrane; Proteomics identification; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

76850.6
Length
665
Aromaticity
0.12
Instability index
40.05
Isoelectric point
6.16
Charge

(pH=7)

-5.94
2D Binding mode
Binding energy

(Kcal/mol)

-8.51
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
RIPLQIVRAETELSAEEKAFLNAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIISLIQNQHYQEVIRNLVKRYVAAMIRNSKTTEENFKELKQDISSFRYEVLDLL
Hydrogen bonds contact
Hydrophobic contact
8Endothelin-converting enzyme 1 (ECE1)3DWB8.34
Target general information
Gen name
ECE1
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
ECE-1
Protein family
Peptidase M13 family
Biochemical class
Peptidase
Function
Converts big endothelin-1 to endothelin-1.
Related diseases
Hirschsprung disease, cardiac defects, and autonomic dysfunction (HCAD) [MIM:613870]: A disorder characterized by skip-lesions Hirschsprung disease, craniofacial abnormalities and other dysmorphic features, cardiac defects including ductus arteriosus, small subaortic ventricular septal defect, small atrial septal defect, and autonomic dysfunction. {ECO:0000269|PubMed:9915973}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07171
Interacts with
P49760; A8MQ03; Q8IUG1; P60370; P60410
EC number
EC 3.4.24.71
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Disease variant; Disulfide bond; Glycoprotein; Hirschsprung disease; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteomics identification; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; Zinc
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

75247.9
Length
660
Aromaticity
0.12
Instability index
46.29
Isoelectric point
5.33
Charge

(pH=7)

-18.3
2D Binding mode
Binding energy

(Kcal/mol)

-8.82
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW
Hydrogen bonds contact
Hydrophobic contact
9Prothrombin4UD98.34
Target general information
Gen name
F2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
Peptidase S1 family
Biochemical class
Hydrolase
Function
Calcium ion binding.Growth factor activity.Heparin binding.Lipopolysaccharide binding.Receptor binding.Serine-type endopeptidase activity.Thrombospondin receptor activity.
Related diseases
Factor II deficiency (FA2D) [MIM:613679]: A very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. {ECO:0000269|PubMed:1349838, ECO:0000269|PubMed:1354985, ECO:0000269|PubMed:1421398, ECO:0000269|PubMed:14962227, ECO:0000269|PubMed:2719946, ECO:0000269|PubMed:3242619, ECO:0000269|PubMed:3567158, ECO:0000269|PubMed:3771562, ECO:0000269|PubMed:3801671, ECO:0000269|PubMed:6405779, ECO:0000269|PubMed:7792730, ECO:0000269|PubMed:7865694}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Thrombophilia due to thrombin defect (THPH1) [MIM:188050]: A multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. {ECO:0000269|PubMed:2825773}. The disease is caused by variants affecting the gene represented in this entry. A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis.; DISEASE: Pregnancy loss, recurrent, 2 (RPRGL2) [MIM:614390]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. {ECO:0000269|PubMed:11506076}. Disease susceptibility is associated with variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07211; DB07796; DB07016; DB07521; DB06850; DB07091; DB06845; DB07088; DB07131; DB07095; DB07515; DB07897; DB06878; DB06947; DB08624; DB06869; DB06929; DB07400; DB04771; DB04772; DB02287; DB07277; DB07550; DB07549; DB07548; DB07105; DB04722; DB07366; DB08254; DB01725; DB08062; DB07639; DB07461; DB07120; DB07190; DB07741; DB07353; DB07508; DB07809; DB08546; DB08061; DB07718; DB03136; DB02723; DB07440; DB07376; DB06861; DB06866; DB06865; DB03865; DB06841; DB07934; DB08422; DB07659; DB07660; DB07658; DB13151; DB00025; DB11166; DB00278; DB01766; DB07083; DB00006; DB00100; DB13152; DB09228; DB09130; DB03159; DB06911; DB06996; DB06919; DB07027; DB07133; DB07143; DB07005; DB06695; DB00055; DB01225; DB05714; DB12831; DB03847; DB07278; DB01767; DB06404; DB09332; DB00001; DB13998; DB04136; DB00170; DB06838; DB13999; DB06868; DB06942; DB06936; DB07165; DB07527; DB07522; DB07665; DB07946; DB06859; DB06853; DB06858; DB07279; DB08187; DB04591; DB07944; DB07128; DB12598; DB01123; DB04786; DB05777; DB04697; DB09109; DB14738; DB04898; DB01593; DB14487; DB08152
Interacts with
P05067; P07204; Q846V4; PRO_0000032489 [P01008]
EC number
3.4.21.5
Uniprot keywords
3D-structure; Acute phase; Blood coagulation; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Disease variant; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; Kringle; Pharmaceutical; Protease; Proteomics identification; Reference proteome; Repeat; Secreted; Serine protease; Signal; Thrombophilia; Zymogen
Protein physicochemical properties
Chain ID
H
Molecular weight

(Da)

29321.6
Length
254
Aromaticity
0.1
Instability index
39.57
Isoelectric point
8.56
Charge

(pH=7)

4.16
2D Binding mode
Binding energy

(Kcal/mol)

-7.45
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
IVEGSDAEIGMSPWQVMLFRSPQELLCGASLISDRWVLTAAHCLLTENDLLVRIGKHSRTRYRNIEKISMLEKIYIHPRYNWENLDRDIALMKLKKPVAFSDYIHPVCLPDRETLLQAGYKGRVTGWGNLKETWGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAYKKRGDACEGDSGGPFVMKSNNRWYQMGIVSWGEGCRDGKYGFYTHVFRLKKWIQKVIDQFGGDFEEIPEELQCGLRPLFEKKSLE
Hydrogen bonds contact
Hydrophobic contact
10Clostridium histolyticum Collagenase (CH colG)7Z5U8.33
Target general information
Gen name
CH colG
Organism
Hathewaya histolytica (Clostridium histolyticum)
Uniprot ID
TTD ID
Synonyms
Microbial collagenase; Gelatinase ColG; Collagenase ColG; Class I collagenase
Protein family
Peptidase M9B family, Collagenase subfamily
Biochemical class
NA
Function
Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen. Active on soluble type I collagen, insoluble collagen, azocoll, soluble PZ-peptide (all collagenase substrates) and gelatin. The full-length protein has collagenase activity, while the in vivo derived C-terminally truncated shorter versions only act on gelatin. In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain are also synergistic with ColH, although their overall efficiency is decreased. The activator domain (residues 119-388) and catalytic subdomain (389-670) open and close around substrate using a Gly-rich hinge (387-397), allowing digestion when the protein is closed. Binding of collagen requires Ca(2+) and is inhibited by EGTA; the collagen-binding domain (CBD, S3a plus S3b) specifically recognizes the triple-helical conformation made by 3 collagen protein chains in the triple-helical region. Isolated CBD (S3a plus S3b) binds collagen fibrils and sheets of many tissues.
Related diseases
Intellectual developmental disorder, X-linked, syndromic, Claes-Jensen type (MRXSCJ) [MIM:300534]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSCJ patients manifest intellectual disability associated with variable features such as slowly progressive spastic paraplegia, seizures, facial dysmorphism. {ECO:0000269|PubMed:15586325, ECO:0000269|PubMed:16538222, ECO:0000269|PubMed:16541399, ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17468742, ECO:0000269|PubMed:23356856, ECO:0000269|PubMed:25666439}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
EC 3.4.24.3
Uniprot keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Pharmaceutical; Protease; Repeat; Secreted; Signal; Virulence; Zinc; Zymogen
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

44751.2
Length
386
Aromaticity
0.15
Instability index
27.33
Isoelectric point
5.77
Charge

(pH=7)

-7.33
2D Binding mode
Binding energy

(Kcal/mol)

-8.83
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
DHDKFLDDAEKHYLPKTYTFDNGTFIIRAGDKVSEEKIKRLYWASREVKSQFHRVVGNDKALEVGNADDVLTMKIFNSPEEYKFNTTDNGGLYIEPRGTFYTYERTPQQSIFSLEELFRHEYTHYLQARYLVDGLWGQGPFYEKNRLTWFDEGTAEFFAGSTRTSGVLPRKLILGYLAKDKVDHRYSLKKTLNSGYDDSDWMFYNYGFAVAHYLYEKDMPTFIKMNKAILNTDVKSYDEIIKKLSDDANKNTEYQNHIQELVDKYQGAGIPLVSDDYLKDHGYKKASEVYSEISKAASLTNTSVTAEKSQYFNTFTLRGTYTGETSKGEFKDWDEMSKKLDGTLESLAKNSWSGYKTLTAYFTNYRVTSDNKVQYDVVFHGVLTDN
Hydrogen bonds contact
Hydrophobic contact
11Enteropeptidase (TMPRSS15)6ZOV8.31
Target general information
Gen name
TMPRSS15
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Transmembrane protease serine 15; TMPRSS15; Serine protease 7; Enterokinase
Protein family
Peptidase S1 family
Biochemical class
Peptidase
Function
Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
Related diseases
Enterokinase deficiency (ENTKD) [MIM:226200]: Life-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive. {ECO:0000269|PubMed:11719902}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
EC 3.4.21.9
Uniprot keywords
3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Lipoprotein; Membrane; Myristate; Protease; Proteomics identification; Reference proteome; Repeat; Serine protease; Signal-anchor; Transmembrane; Transmembrane helix; Zymogen
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

26220.3
Length
234
Aromaticity
0.1
Instability index
50.13
Isoelectric point
4.82
Charge

(pH=7)

-9.93
2D Binding mode
Binding energy

(Kcal/mol)

-8.01
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
IVGGSDAKEGAWPWVVGLYYDDRLLCGASLVSSDWLVSAAHCVYGRNLEPSKWTAILGLHMKSNLTSPQTVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPISLPEENQVFPPGRNCSIAGWGTVVYQGTTADILQEADVPLLSNERCQQQMPEYNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYECALPNRPGVYARVSRFTEWIQSFL
Hydrogen bonds contact
Hydrophobic contact
12Macrophage colony-stimulating factor 1 receptor (CSF1R)2I1M8.29
Target general information
Gen name
CSF1R
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Proto-oncogene c-Fms; M-CSF-R; FMS; CSF-1R; CSF-1-R; CSF-1 receptor; CD115
Protein family
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
Biochemical class
Kinase
Function
Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes.
Related diseases
Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.; DISEASE: Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.; DISEASE: Leukoencephalopathy, hereditary diffuse, with spheroids 1 (HDLS1) [MIM:221820]: An autosomal dominant adult-onset rapidly progressive neurodegenerative disorder characterized by variable behavioral, cognitive, and motor changes. Patients often die of dementia within 6 years of onset. Brain imaging shows patchy abnormalities in the cerebral white matter, predominantly affecting the frontal and parietal lobes. {ECO:0000269|PubMed:22197934, ECO:0000269|PubMed:23408870, ECO:0000269|PubMed:24336230, ECO:0000269|PubMed:24532199}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Brain abnormalities, neurodegeneration, and dysosteosclerosis (BANDDOS) [MIM:618476]: An autosomal recessive disease with variable manifestations. Main features are brain malformations with calcifying leukoencephalopathy, progressive neurodegeneration, and bone sclerotic features. The age at onset ranges from infancy to early adulthood. Neurologic features include loss of previous motor and language skills, cognitive impairment, spasticity, and focal seizures. Brain imaging shows periventricular white matter abnormalities and calcifications, large cisterna magna or Dandy-Walker malformation, and sometimes agenesis of the corpus callosum. {ECO:0000269|PubMed:30982608, ECO:0000269|PubMed:30982609}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07167; DB07202; DB12147; DB12010; DB00619; DB06080; DB12978; DB01268
Interacts with
P09603; Q15375; P29323; Q6ZMJ4-1
EC number
EC 2.7.10.1
Uniprot keywords
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Disease variant; Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Inflammatory response; Innate immunity; Kinase; Membrane; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Proteomics identification; Proto-oncogene; Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

35082.9
Length
311
Aromaticity
0.11
Instability index
44.6
Isoelectric point
8.13
Charge

(pH=7)

2.42
2D Binding mode
Binding energy

(Kcal/mol)

-9.26
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
QVRWKIIESYNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKSRVLETDSTASTRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRER
Hydrogen bonds contact
Hydrophobic contact
13Fatty acid synthase (FASN)3TJM8.27
Target general information
Gen name
FASN
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Yeast fatty acid synthase; Fatty-acyl-CoA synthase; Fatty acyl-CoA synthetase enzyme; FAS
Protein family
NA
Biochemical class
Acyltransferase
Function
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein.
Related diseases
Glycine encephalopathy 2 (GCE2) [MIM:620398]: A form of glycine encephalopathy, a metabolic disorder characterized by a high concentration of glycine in the body fluids. Affected individuals typically have severe neurological symptoms, including seizure, lethargy, and muscular hypotonia soon after birth. Most of them die within the neonatal period. Atypical cases have later disease onset and less severely affected psychomotor development. {ECO:0000269|PubMed:10873393, ECO:0000269|PubMed:11286506, ECO:0000269|PubMed:16051266, ECO:0000269|PubMed:26371980, ECO:0000269|PubMed:28244183, ECO:0000269|PubMed:8005589, ECO:0000269|PubMed:9600239, ECO:0000269|PubMed:9621520}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01034; DB01083
Interacts with
Q15848; Q16665; P42858; Q8IV20; Q8TBB1; PRO_0000045603 [Q99IB8]
EC number
EC 2.3.1.85
Uniprot keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase; Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein; Proteomics identification; Pyridoxal phosphate; Reference proteome; S-nitrosylation; Transferase; Ubl conjugation
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

30174.9
Length
275
Aromaticity
0.09
Instability index
43.28
Isoelectric point
5.92
Charge

(pH=7)

-5.4
2D Binding mode
Binding energy

(Kcal/mol)

-9.54
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
NLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTGSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAAAGADYNLSQVCDGKVSVHVIEGDHATLLEGSGLESIISIIHSS
Hydrogen bonds contact
Hydrophobic contact
14Lanosterol 14-alpha demethylase (CYP51A1)4UHI8.25
Target general information
Gen name
CYP51A1
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Cytochrome P450LI; Cytochrome P45014DM; Cytochrome P450-14DM; Cytochrome P450 51A1
Protein family
Cytochrome P450 family
Biochemical class
Cytochrome P450 family
Function
Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
Related diseases
Spondyloepimetaphyseal dysplasia, short limb-hand type (SEMD-SL) [MIM:271665]: A bone disease characterized by short-limbed dwarfism, a narrow chest with pectus excavatum, brachydactyly in the hands and feet, a characteristic craniofacial appearance and premature calcifications. The radiological findings are distinctive and comprise short long bones throughout the skeleton with striking epiphyses that are stippled, flattened and fragmented and flared, irregular metaphyses. Platyspondyly in the spine with wide intervertebral spaces is observed and some vertebral bodies are pear-shaped with central humps, anterior protrusions and posterior scalloping. {ECO:0000269|PubMed:19110212, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:26463668}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Warburg-Cinotti syndrome (WRCN) [MIM:618175]: An autosomal dominant disease characterized by progressive corneal neovascularization, keloid formation, chronic skin ulcers, wasting of subcutaneous tissue, flexion contractures of the fingers, and acro-osteolysis. {ECO:0000269|PubMed:30449416}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07705; DB05667; DB01110; DB01007
Interacts with
NA
EC number
EC 1.14.14.154
Uniprot keywords
3D-structure; Alternative splicing; Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum; Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Proteomics identification; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A,B,C,D
Molecular weight

(Da)

53013.3
Length
462
Aromaticity
0.11
Instability index
47.66
Isoelectric point
8.8
Charge

(pH=7)

7
2D Binding mode
Binding energy

(Kcal/mol)

-8.42
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDLNLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSLPGWLPLPSFRRRDRAHREI
Hydrogen bonds contact
Hydrophobic contact
15Dopamine beta-hydroxylase4ZEL8.25
Target general information
Gen name
DBH
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
Copper type II ascorbate-dependent monooxygenase family
Biochemical class
Oxidoreductase
Function
Catalytic activity.Copper ion binding.Dopamine beta-monooxygenase activity.L-ascorbic acid binding.
Related diseases
Orthostatic hypotension 1 (ORTHYP1) [MIM:223360]: A form of orthostatic hypotension due to congenital dopamine beta-hydroxylase deficiency. Orthostatic hypotension, also known as postural hypotension, is a finding defined as a 20-mm Hg decrease in systolic pressure or a 10-mm Hg decrease in diastolic pressure occurring 3 minutes after a person has risen from supine to standing. Symptoms include dizziness, blurred vision, and sometimes syncope. ORTHYP1 is an autosomal recessive condition apparent from infancy or early childhood and characterized by low plasma and urinary levels of norepinephrine and epinephrine, and episodic hypoglycemia. {ECO:0000269|PubMed:11857564}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00126; DB06774; DB09130; DB05394; DB00822; DB00988; DB00968; DB00550
Interacts with
P00352; P63010-2; Q04656; Q8WUW1; Q9UNS2; Q71DI3; P61978; Q9Y2M5; Q92876; P08727; Q14693; P0DPK4; Q6GQQ9-2; P27986-2; Q9ULX5; Q96D59; Q8N6K7-2; Q9GZS3; Q8IUW3; Q86WT6-2
EC number
1.14.17.1
Uniprot keywords
3D-structure; Catecholamine biosynthesis; Copper; Cytoplasmic vesicle; Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Proteomics identification; Reference proteome; Secreted; Signal-anchor; Transmembrane; Transmembrane helix; Vitamin C
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

123694
Length
1094
Aromaticity
0.1
Instability index
51.85
Isoelectric point
5.84
Charge

(pH=7)

-24.5
2D Binding mode
Binding energy

(Kcal/mol)

-8.54
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTVVSPLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEVPHFSGPCDSKMLNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCVVSIGG
Hydrogen bonds contact
Hydrophobic contact
16Retinoic acid receptor RXR-beta (RXRB)5HJP8.21
Target general information
Gen name
RXRB
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Retinoid X receptor beta; Nuclear receptor subfamily 2 group B member 2; NR2B2
Protein family
Nuclear hormone receptor family, NR2 subfamily
Biochemical class
Nuclear hormone receptor
Function
Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE). Receptor for retinoic acid.
Related diseases
Noonan syndrome 13 (NS13) [MIM:619087]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. NS13 inheritance is autosomal dominant. There is considerable variability in severity. {ECO:0000269|PubMed:32721402}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB08175; DB00459; DB00210; DB00523; DB00307; DB01393; DB03756; DB00926; DB01941; DB07929; DB02746; DB00412; DB00799; DB07080; DB00755
Interacts with
Q00975; Q9HB07; F1D8P7; Q13133; Q13133-3; Q96RI1-1; P04150; Q9NRD5; P37231; P10276; P10276-2; P10826-2; P13631; Q6IQ16; Q13137; Q96B26; Q08379; Q6A162; Q9UJV3-2; Q13133-3; Q96RI1-1; O43586; P10276; P10826-2; Q8IUQ4-2; O75528; Q12800; Q9UBB9; Q05BL1; P14373; O94972; Q96S82
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Methylation; Nucleus; Proteomics identification; Receptor; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
A,C
Molecular weight

(Da)

28845.8
Length
251
Aromaticity
0.08
Instability index
54.86
Isoelectric point
6.74
Charge

(pH=7)

-0.6
2D Binding mode
Binding energy

(Kcal/mol)

-9.73
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
QLTAAQELMIQQLVAAQLQCNKRSFSDQPKVTPWPSASQQRFAHFTELAIISVQEIVDFAKQVPGFLQLGREDQIALLKASTIEIMLLETARRYNHETECITFLKDFTYSKDDFHRAGLQVEFINPIFEFSRAMRRLGLDDAEYALLIAINIFSADRPNVQEPGRVEALQQPYVEALLSYTRIKRPQDQLRFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHEGSGSGSHKILHRLLQD
Hydrogen bonds contact
Hydrophobic contact
17Multidrug resistance protein 3 (ABCB4)6S7P8.20
Target general information
Gen name
ABCB4
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
PGY3; MDR3; ATP-binding cassette sub-family B member 4; ABCB4
Protein family
ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily
Biochemical class
Acid anhydrides hydrolase
Function
Mediates ATP-dependent export of organic anions and drugs from the cytoplasm. Hydrolyzes ATP with low efficiency. Not capable of conferring drug resistance. Mediates the translocation of phosphatidylcholine across the canalicular membrane of the hepatocyte.
Related diseases
Cholestasis, progressive familial intrahepatic, 3 (PFIC3) [MIM:602347]: A disorder characterized by early onset of cholestasis that progresses to hepatic fibrosis, cirrhosis, and end-stage liver disease before adulthood. PFIC3 inheritance is autosomal recessive. {ECO:0000269|PubMed:11313315, ECO:0000269|PubMed:12671900, ECO:0000269|PubMed:17726488, ECO:0000269|PubMed:21119540, ECO:0000269|PubMed:24045840, ECO:0000269|PubMed:24594635, ECO:0000269|PubMed:24806754, ECO:0000269|PubMed:28012258, ECO:0000269|PubMed:9419367}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cholestasis of pregnancy, intrahepatic 3 (ICP3) [MIM:614972]: A liver disorder of pregnancy. It presents during the second or, more commonly, the third trimester of pregnancy with intense pruritus which becomes more severe with advancing gestation and cholestasis. It causes fetal distress, spontaneous premature delivery and intrauterine death. Patients have spontaneous and progressive disappearance of cholestasis after delivery. Cholestasis results from abnormal biliary transport from the liver into the small intestine. {ECO:0000269|PubMed:10767346, ECO:0000269|PubMed:12746424, ECO:0000269|PubMed:15077010}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Gallbladder disease 1 (GBD1) [MIM:600803]: One of the major digestive diseases. Gallstones composed of cholesterol (cholelithiasis) are the common manifestations in western countries. Most people with gallstones, however, remain asymptomatic through their lifetimes. {ECO:0000269|PubMed:11313316, ECO:0000269|PubMed:12891548, ECO:0000269|PubMed:22331132, ECO:0000269|PubMed:23533021, ECO:0000269|PubMed:24723470, ECO:0000269|PubMed:28012258, ECO:0000269|PubMed:28587926, ECO:0000269|Ref.2}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB06414; DB06207
Interacts with
NA
EC number
EC 7.6.2.1
Uniprot keywords
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle; Disease variant; Glycoprotein; Intrahepatic cholestasis; Lipid transport; Membrane; Nucleotide-binding; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Translocase; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

123919
Length
1128
Aromaticity
0.1
Instability index
29.44
Isoelectric point
8.78
Charge

(pH=7)

11.08
2D Binding mode
Binding energy

(Kcal/mol)

-8.92
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
VLTLFRYSDWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDKPGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDQATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNVPPVSFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDQATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVK
Hydrogen bonds contact
Hydrophobic contact
18Purine nucleoside phosphorylase (PNP)4EAR8.20
Target general information
Gen name
PNP
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
PNP; Inosine phosphorylase
Protein family
PNP/MTAP phosphorylase family
Biochemical class
Pentosyltransferase
Function
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Related diseases
Purine nucleoside phosphorylase deficiency (PNPD) [MIM:613179]: A disorder that interrupts both the catabolism of inosine into hypoxanthine and guanosine into guanine, and leads to the accumulation of guanosine, inosine, and their deoxified by-products. The main clinical presentation is recurrent infections due to severe T-cell immunodeficiency. Some patients also have neurologic impairment. {ECO:0000269|PubMed:1384322, ECO:0000269|PubMed:3029074, ECO:0000269|PubMed:8931706}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB03881; DB03551; DB02222; DB02391; DB03609; DB01667; DB04260; DB02796; DB04753; DB00640; DB00242; DB00900; DB06185; DB02377; DB02857; DB04754; DB04757; DB04076; DB02230; DB04335; DB02568; DB03101
Interacts with
P05067; Q9UQM7; O14576-2; P06241; P14136; Q92993-2; Q9BXM7; P00491; P17612; P63000; Q92673; Q15583
EC number
EC 2.4.2.1
Uniprot keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Disease variant; Glycosyltransferase; Phosphoprotein; Proteomics identification; Purine salvage; Reference proteome; Transferase
Protein physicochemical properties
Chain ID
A,B,C
Molecular weight

(Da)

31849.2
Length
288
Aromaticity
0.1
Instability index
34.77
Isoelectric point
6.42
Charge

(pH=7)

-1.63
2D Binding mode
Binding energy

(Kcal/mol)

-9.71
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GYTYEDYKNTAEYLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTYKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANXEEVLAAGKQAAQKLEQFVSILMASIDRFPAMSDA
Hydrogen bonds contact
Hydrophobic contact
19Platelet glycoprotein VI (GP6)5OU78.19
Target general information
Gen name
GP6
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Glycoprotein 6; GPVI
Protein family
NA
Biochemical class
NA
Function
Collagen receptor involved in collagen-induced platelet adhesion and activation. Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma-chain, the Src kinases (likely FYN or LYN) and SYK, the adapter protein LAT and leads to the activation of PLCG2.
Related diseases
Bleeding disorder, platelet-type, 11 (BDPLT11) [MIM:614201]: A mild to moderate bleeding disorder caused by defective platelet activation and aggregation in response to collagen. {ECO:0000269|PubMed:19549989, ECO:0000269|PubMed:19552682}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
P06241; P07948; P06241; P07948
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Blood coagulation; Cell membrane; Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; Hemostasis; Immunoglobulin domain; Membrane; Proteomics identification; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

19027.4
Length
173
Aromaticity
0.11
Instability index
37.14
Isoelectric point
8.68
Charge

(pH=7)

2.52
2D Binding mode
Binding energy

(Kcal/mol)

-6.86
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAMKRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGSGGDVTLQCQTRYGFDQFALYKEGDPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTG
Hydrogen bonds contact
Hydrophobic contact
20Kallikrein-4 (KLK4)7JOW8.13
Target general information
Gen name
KLK4
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Serine protease 17; Prostase; PSTS; PRSS17; Kallikreinlike protein 1; Kallikrein4; Kallikrein-like protein 1; KLKL1; KLK-L1; Enamel matrix serine proteinase 1; EMSP1
Protein family
Peptidase S1 family, Kallikrein subfamily
Biochemical class
Peptidase
Function
Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix. Has a major role in enamel formation.
Related diseases
Amelogenesis imperfecta, hypomaturation type, 2A1 (AI2A1) [MIM:204700]: A defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel. {ECO:0000269|PubMed:15235027}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
P20155; Q06418
EC number
EC 3.4.21.-
Uniprot keywords
3D-structure; Alternative splicing; Amelogenesis imperfecta; Biomineralization; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease; Proteomics identification; Reference proteome; Secreted; Serine protease; Signal; Zinc; Zymogen
Protein physicochemical properties
Chain ID
E,I
Molecular weight

(Da)

41763.9
Length
387
Aromaticity
0.07
Instability index
32.75
Isoelectric point
5.38
Charge

(pH=7)

-11.36
2D Binding mode
Binding energy

(Kcal/mol)

-8.71
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
IINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIGLGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGGQDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQAGSSVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRFESPLRINIIKESYFLNIKFGPSSSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGEGYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRKAT
Hydrogen bonds contact
Hydrophobic contact