Job Results:

Ligand

Structure

Job ID

fa349302d5037e2532241dc19bc07bba

Job name

NA

Time

2026-10-04 08:54:01

Rank Target PDB ID AirScore Detail
1Zinc finger protein Helios (IKZF2)7LPS6.33
Target general information
Gen name
IKZF2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Ikaros family zinc finger protein 2
Protein family
Ikaros C2H2-type zinc-finger protein family
Biochemical class
NA
Function
Associates with Ikaros at centromeric heterochromatin.
Related diseases
Developmental and epileptic encephalopathy 25, with amelogenesis imperfecta (DEE25) [MIM:615905]: An autosomal recessive disease characterized by subclinical seizures appearing in the first days of life, evolving to severe epileptic disease. Affected individuals have profound or severe delayed development with lack of speech, and most patients do not acquire the ability to sit. Additional variable features include axial hypotonia, peripheral hypertonia, and abnormal involuntary movements such as dystonia and choreoathetosis. Dental abnormalities, including delayed eruption, hypodontia, tooth hypoplasia, yellow discoloration, thin enamel, and enamel chipping are observed in most patients. {ECO:0000269|PubMed:24995870, ECO:0000269|PubMed:26384929, ECO:0000269|PubMed:30054523}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
P29972; P56545; P56545-3; Q17RB8; P09022; Q8N8B7-2
EC number
NA
Uniprot keywords
3D-structure; Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
B,C
Molecular weight

(Da)

47006.6
Length
410
Aromaticity
0.09
Instability index
44.28
Isoelectric point
7.23
Charge

(pH=7)

0.69
2D Binding mode
Binding energy

(Kcal/mol)

-8.64
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
INFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDGERPFHCNQCGASFTQKGNLLRHIKLHSG
Hydrogen bonds contact
Hydrophobic contact
2Neuronal acetylcholine receptor alpha-2 (CHRNA2)5FJV6.29
Target general information
Gen name
CHRNA2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
CHRNA2
Protein family
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-2/CHRNA2 sub-subfamily
Biochemical class
Neurotransmitter receptor
Function
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Related diseases
Epilepsy, nocturnal frontal lobe, 4 (ENFL4) [MIM:610353]: An autosomal dominant focal epilepsy characterized by nocturnal seizures associated with fear sensation, tongue movements, and nocturnal wandering, closely resembling nightmares and sleep walking. {ECO:0000269|PubMed:16826524}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Seizures, benign familial infantile, 6 (BFIS6) [MIM:610353]: A form of benign familial infantile epilepsy, a neurologic disorder characterized by afebrile seizures occurring in clusters during the first year of life, without neurologic sequelae. BFIS6 inheritance is autosomal dominant. {ECO:0000269|PubMed:25847220}. The disease may be caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00732; DB00237; DB00411; DB00565; DB01245; DB00514; DB01135; DB07720; DB00898; DB00472; DB00483; DB08960; DB00657; DB01336; DB00416; DB01226; DB00184; DB01337; DB01338; DB00721; DB00728; DB05740; DB00202; DB01199; DB01339
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Disease variant; Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

48323.4
Length
413
Aromaticity
0.15
Instability index
32
Isoelectric point
5.69
Charge

(pH=7)

-6.58
2D Binding mode
Binding energy

(Kcal/mol)

-8.57
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
DRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLP
Hydrogen bonds contact
Hydrophobic contact
34-hydroxyphenylpyruvate dioxygenase3ISQ6.25
Target general information
Gen name
HPD
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
PPD
Protein family
4HPPD family
Biochemical class
Oxidoreductase
Function
4-hydroxyphenylpyruvate dioxygenase activity.Metal ion binding.
Related diseases
Tyrosinemia 3 (TYRSN3) [MIM:276710]: An inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, seizures and mild intellectual disability. {ECO:0000269|PubMed:10942115, ECO:0000269|PubMed:11073718}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hawkinsinuria (HWKS) [MIM:140350]: An inborn error of tyrosine metabolism characterized by failure to thrive, persistent metabolic acidosis, fine and sparse hair, and excretion of the unusual cyclic amino acid metabolite, hawkinsin, in the urine. {ECO:0000269|PubMed:11073718}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB02850; DB00348
Interacts with
NA
EC number
1.13.11.27
Uniprot keywords
3D-structure; Acetylation; Alternative splicing; Cytoplasm; Dioxygenase; Disease variant; Endoplasmic reticulum; Golgi apparatus; Intellectual disability; Iron; Membrane; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Tyrosine catabolism
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

43164.8
Length
376
Aromaticity
0.11
Instability index
32.38
Isoelectric point
6.73
Charge

(pH=7)

-1.04
2D Binding mode
Binding energy

(Kcal/mol)

-8.53
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
AKPERGRFLHFHSVTFWVGNAKQAASFYCSKMGFEPLAYRGLETGSREVVSHVIKQGKIVFVLSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMREPWVEQDKFGKVKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEMIDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGLEFLSVPSTYYKQLREKLKTAKIKVKENIDALEELKILVDYDEKGYLLQIFTKPVQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQNLRGNLTNM
Hydrogen bonds contact
Hydrophobic contact
4Protein cereblon (CRBN)5FQD6.23
Target general information
Gen name
CRBN
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Protein cereblon
Protein family
CRBN family
Biochemical class
NA
Function
Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. May play a role in memory and learning by regulating the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1. Binding of pomalidomide and other thalidomide-related drugs changes the substrate specificity of the human protein, leading to decreased degradation of MEIS2 and other target proteins and increased degradation of MYC, IRF4, IKZF1 and IKZF3.
Related diseases
Intellectual developmental disorder, autosomal recessive 2 (MRT2) [MIM:607417]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT2 patients display mild intellectual disability with a standard IQ ranged from 50 to 70. IQ scores are lower in males than females. Developmental milestones are mildly delayed. There are no dysmorphic or autistic features. {ECO:0000269|PubMed:15557513, ECO:0000269|PubMed:28143899}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00480; DB08910; DB01041
Interacts with
Q96A83-2; P48729; Q16531; O14901; Q8IVT2; Q9P286; A0A6Q8PF08; Q93062; Q16531; Q13422-7
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cytoplasm; Disease variant; Intellectual disability; Membrane; Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc
Protein physicochemical properties
Chain ID
B,E
Molecular weight

(Da)

38245.7
Length
337
Aromaticity
0.08
Instability index
40.62
Isoelectric point
5.7
Charge

(pH=7)

-6.53
2D Binding mode
Binding energy

(Kcal/mol)

-8.5
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
EFIVGGKYKLNITNGEEVAVINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEIVKVKAIGRQRFKVLEQQAKVQILPECVLAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPD
Hydrogen bonds contact
Hydrophobic contact
5Matrix metalloproteinase-16 (MMP-16)1RM86.22
Target general information
Gen name
MMP16
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Membrane-type-3 matrix metalloproteinase; Membrane-type matrix metalloproteinase 3; MTMMP3; MT3MMP; MT3-MMP; MT-MMP 3; MMPX2; MMP-X2; C8orf57
Protein family
Peptidase M10A family
Biochemical class
Peptidase
Function
Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells. Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin.
Related diseases
Cerebral creatine deficiency syndrome 3 (CCDS3) [MIM:612718]: An autosomal recessive disorder characterized by developmental delay/regression, intellectual disability, severe disturbance of expressive and cognitive speech, and severe depletion of creatine/phosphocreatine in the brain. Most patients develop a myopathy characterized by muscle weakness and atrophy later in life. {ECO:0000269|PubMed:11555793, ECO:0000269|PubMed:20682460, ECO:0000269|PubMed:22386973, ECO:0000269|PubMed:23660394, ECO:0000269|PubMed:23770102, ECO:0000269|PubMed:26490222, ECO:0000269|PubMed:27233232}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fanconi renotubular syndrome 1 (FRTS1) [MIM:134600]: A form of Fanconi renotubular syndrome, a disease due to a generalized dysfunction of the proximal kidney tubule resulting in decreased solute and water reabsorption. Patients have polydipsia and polyuria with phosphaturia, glycosuria and aminoaciduria. They may develop hypophosphatemic rickets or osteomalacia, acidosis and a tendency toward dehydration. Some eventually develop renal insufficiency. FRTS1 inheritance is autosomal dominant. {ECO:0000269|PubMed:29654216}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB03880; DB00786
Interacts with
NA
EC number
EC 3.4.24.-
Uniprot keywords
3D-structure; Alternative splicing; Calcium; Cell membrane; Cleavage on pair of basic residues; Collagen degradation; Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Proteomics identification; Reference proteome; Repeat; Secreted; Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

18853.6
Length
169
Aromaticity
0.12
Instability index
33.65
Isoelectric point
4.88
Charge

(pH=7)

-12.42
2D Binding mode
Binding energy

(Kcal/mol)

-8.48
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGP
Hydrogen bonds contact
Hydrophobic contact
6Neuronal acetylcholine receptor subunit alpha-34ZK46.21
Target general information
Gen name
CHRNA3
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
NACHRA3
Protein family
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-3/CHRNA3 sub-subfamily
Biochemical class
Acetylcholine binding protein
Function
Acetylcholine binding.Acetylcholine-gated cation-selective channel activity.Acetylcholine receptor activity.Ligand-gated ion channel activity.Serotonin-gated cation-selective channel activity.
Related diseases
Bladder dysfunction, autonomic, with impaired pupillary reflex and secondary CAKUT (BAIPRCK) [MIM:191800]: An autosomal recessive disease characterized by impaired innervation and autonomic dysfunction of the urinary bladder, hydronephrosis, vesicoureteral reflux, small kidneys, recurrent urinary tract infections, and progressive renal insufficiency. Additional autonomic features are impaired pupillary reflex and orthostatic hypotension. The disease manifests in utero or early childhood. {ECO:0000269|PubMed:31708116}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00915; DB01156; DB00237; DB00565; DB09028; DB00514; DB07720; DB00898; DB00472; DB05710; DB01227; DB00848; DB00333; DB00184; DB01090; DB00202; DB01273
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Disease variant; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Phosphoprotein; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix; Transport; Ubl conjugation
Protein physicochemical properties
Chain ID
A,B,C,D,E
Molecular weight

(Da)

46391.5
Length
408
Aromaticity
0.12
Instability index
30.23
Isoelectric point
4.6
Charge

(pH=7)

-22.73
2D Binding mode
Binding energy

(Kcal/mol)

-8.47
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
LHSQANLMRLKSDLFYPGPTKDDPLTVTLGFTLQDIVKADSSTNEVDLVYWEQQRWKLNSLMWDPNEYGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQRLSFMCDPTGVDSEEGATCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQYKHDIKYNCCEEIYPDVVLVVKFRERRLHSQANLMRLKSDLFNRYPGPTKDDPLTVTLGFTLQDIVKADSSTNEVDLVYWEQQRWKLNSLMWDPNEYGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQRLSFMCDPTGVDSEEGATCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQYKHDIKYNCCEEIYPDVVLVVKFRE
Hydrogen bonds contact
Hydrophobic contact
7Cytochrome c oxidase subunit 23VRJ6.20
Target general information
Gen name
MT-CO2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
MTCO2;COXII;COII;COX2
Protein family
Cytochrome c oxidase subunit 2 family
Biochemical class
Immune system
Function
Copper ion binding.Cytochrome-c oxidase activity.
Related diseases
Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and intellectual disability. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:10486321}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB02659; DB04464; DB05412
Interacts with
Q9NZ94-2; P49281-3
EC number
7.1.1.9
Uniprot keywords
3D-structure; Copper; Disease variant; Electron transport; Magnesium; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Primary mitochondrial disease; Proteomics identification; Reference proteome; Respiratory chain; Translocase; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
C
Molecular weight

(Da)

21687.9
Length
189
Aromaticity
0.11
Instability index
38
Isoelectric point
5.68
Charge

(pH=7)

-3.26
2D Binding mode
Binding energy

(Kcal/mol)

-8.46
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRMAPRAPWIEQEGPEYWDGETRNMKASAQTYRENLRIALRYYNQSEAGSHIIQVMYGCDVGPDGRLLRGHDQSAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVEWLRRYLENGKETLQLTTKLTNTNI
Hydrogen bonds contact
Hydrophobic contact
8Caspase-7 (CASP7)1SHJ6.20
Target general information
Gen name
CASP7
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
MCH3; ICE-like apoptotic protease 3; ICE-LAP3; CMH-1; CASP-7; Apoptotic protease Mch-3
Protein family
Peptidase C14A family
Biochemical class
Peptidase
Function
Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. Involved in the activation cascade of caspases responsible for apoptosis execution.
Related diseases
Pregnancy loss, recurrent, 3 (RPRGL3) [MIM:614391]: 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:17339269}. Disease susceptibility is associated with variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB05408; DB03384; DB06255
Interacts with
Q13490; P83105; P42858; Q8N4N3-2; P43364; Q16236; Q9GZT8; Q13177; P27986-2; P21673; Q86WV1-2; P17405; P98170
EC number
EC 3.4.22.60
Uniprot keywords
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; Apoptosis; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease; Proteomics identification; Reference proteome; RNA-binding; Secreted; Thiol protease; Ubl conjugation; Zymogen
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

47441.5
Length
417
Aromaticity
0.11
Instability index
20.98
Isoelectric point
8.38
Charge

(pH=7)

6.12
2D Binding mode
Binding energy

(Kcal/mol)

-8.46
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
TYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGARCKTLLEKPKLFFIQACRGTEPRYKIPVEADFLFAYSTVRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFKKQIPCVVSMLTKELYFSQVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGARCKTLLEKPKLFFIQACRGPRYKIPVEADFLFAYSTVPGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESKQIPCVVSMLTKELYFSQ
Hydrogen bonds contact
Hydrophobic contact
9Helicobacter pylori Methylthioadenosine nucleosidase (HELPY mtnN)4BMZ6.20
Target general information
Gen name
HELPY mtnN
Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Uniprot ID
TTD ID
Synonyms
MTAN; MTA/SAH nucleosidase; Aminofutalosine nucleosidase; Aminodeoxyfutalosine nucleosidase; AFL nucleosidase; 6-amino-6-deoxyfutalosine N-ribosylhydrolase; 5'-methylthioadenosine/S-adenosylhomocystei
Protein family
PNP/UDP phosphorylase family
Biochemical class
NA
Function
Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Can also probably catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2. Does not act on futalosine (FL) as substrate.
Related diseases
Progressive familial heart block 1B (PFHB1B) [MIM:604559]: A cardiac bundle branch disorder characterized by progressive alteration of cardiac conduction through the His-Purkinje system, with a pattern of a right bundle-branch block and/or left anterior hemiblock occurring individually or together. It leads to complete atrio-ventricular block causing syncope and sudden death. {ECO:0000269|PubMed:19726882, ECO:0000269|PubMed:20562447, ECO:0000269|PubMed:21887725}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Erythrokeratodermia variabilis et progressiva 6 (EKVP6) [MIM:618531]: A form of erythrokeratodermia variabilis et progressiva, a genodermatosis characterized by the coexistence of two independent skin lesions: transient erythema and hyperkeratosis that is usually localized but occasionally occurs in its generalized form. Clinical presentation varies significantly within a family and from one family to another. Palmoplantar keratoderma is present in around 50% of cases. EKVP6 inheritance is autosomal dominant. {ECO:0000269|PubMed:30528822}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Amino-acid biosynthesis; Hydrolase; Menaquinone biosynthesis; Methionine biosynthesis; Reference proteome
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

50547.6
Length
464
Aromaticity
0.08
Instability index
26.92
Isoelectric point
5.13
Charge

(pH=7)

-20.92
2D Binding mode
Binding energy

(Kcal/mol)

-8.46
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
VQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPESAIFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSKERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISNNADEEANMSFDAFLEKSAQTSAKFLKSMVDELGSHMVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPESAIFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSKERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISNNADEEANMSFDAFLEKSAQTSAKFLKSMVDEL
Hydrogen bonds contact
Hydrophobic contact
10Acetylcholine receptor subunit alpha4ZJS6.18
Target general information
Gen name
CHRNA1
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
ACHRA;CHNRA
Protein family
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-1/CHRNA1 sub-subfamily
Biochemical class
Immune system
Function
Acetylcholine binding.Acetylcholine-gated cation-selective channel activity.Acetylcholine receptor activity.Ion channel activity.Ligand-gated ion channel activity.
Related diseases
Multiple pterygium syndrome, lethal type (LMPS) [MIM:253290]: Multiple pterygia are found infrequently in children with arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal multiple pterygium syndrome there is intrauterine growth retardation, multiple pterygia, and flexion contractures causing severe arthrogryposis and fetal akinesia. Subcutaneous edema can be severe, causing fetal hydrops with cystic hygroma and lung hypoplasia. Oligohydramnios and facial anomalies are frequent. {ECO:0000269|PubMed:18252226}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: The alpha subunit is the main focus for antibody binding in myasthenia gravis. Myasthenia gravis is characterized by sporadic muscular fatigability and weakness, occurring chiefly in muscles innervated by cranial nerves, and characteristically improved by cholinesterase-inhibiting drugs.; DISEASE: Myasthenic syndrome, congenital, 1A, slow-channel (CMS1A) [MIM:601462]: A common congenital myasthenic syndrome. Congenital myasthenic syndromes are characterized by muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS1A is a slow-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in prolonged AChR channel opening episodes, prolonged endplate currents, and depolarization block. This is associated with calcium overload, which may contribute to subsequent degeneration of the endplate and postsynaptic membrane. {ECO:0000269|PubMed:16685696, ECO:0000269|PubMed:7619526, ECO:0000269|PubMed:8872460, ECO:0000269|PubMed:9158151, ECO:0000269|PubMed:9221765}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 1B, fast-channel (CMS1B) [MIM:608930]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS1B is a fast-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in brief opening and activity of the channel, with a rapid decay in endplate current, failure to achieve threshold depolarization of the endplate and consequent failure to fire an action potential. {ECO:0000269|PubMed:10195214, ECO:0000269|PubMed:12588888, ECO:0000269|PubMed:15079006}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB08838; DB00565; DB00555
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Congenital myasthenic syndrome; Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
A,B,C,D,E
Molecular weight

(Da)

46717.8
Length
411
Aromaticity
0.11
Instability index
38.02
Isoelectric point
4.77
Charge

(pH=7)

-22.31
2D Binding mode
Binding energy

(Kcal/mol)

-8.44
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
EHETRLVAKLFKDYSSVVRPVEDHRQVVEVTLGFTLQDIVKADSSTNEVDLVYYEQQRWVDYNLKWNPDDYGGVKKIHIPAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQRLSFMCDPTGVDSEEGATCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVVKFREEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTLGFTLQDIVKADSSTNEVDLVYYEQQRWVDYNLKWNPDDYGGVKKIHIPAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQRLSFMCDPTGVDSEEGATCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVVKFRER
Hydrogen bonds contact
Hydrophobic contact
11Peptostreptococcal albumin-binding protein2VDB6.18
Target general information
Gen name
pab
Organism
Finegoldia magna (Peptostreptococcus magnus)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
NA
Biochemical class
Protein binding
Function
Binds serum albumin.
Related diseases
LTC4 synthase deficiency is associated with a neurometabolic developmental disorder characterized by muscular hypotonia, psychomotor retardation, failure to thrive, and microcephaly. {ECO:0000269|PubMed:10896305, ECO:0000269|PubMed:9820300}.
Drugs

(DrugBank ID)

DB03600; DB00788
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Cell wall; Peptidoglycan-anchor; Secreted; Signal
Protein physicochemical properties
Chain ID
B
Molecular weight

(Da)

21751.6
Length
189
Aromaticity
0.1
Instability index
49.17
Isoelectric point
5.44
Charge

(pH=7)

-6.7
2D Binding mode
Binding energy

(Kcal/mol)

-8.44
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
EVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLK
Hydrogen bonds contact
Hydrophobic contact
12Opioid receptor sigma 1 (OPRS1)5HK16.18
Target general information
Gen name
SIGMAR1
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
hSigmaR1; Sigma1R; Sigma1-receptor; Sigma non-opioid intracellular receptor 1; Sigma 1-type opioid receptor; SRBP; SR31747-binding protein; SR31747 binding protein 1; SR-BP; SIG-1R; Opioid receptor, s
Protein family
ERG2 family
Biochemical class
GPCR rhodopsin
Function
Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112. Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane.
Related diseases
Amyotrophic lateral sclerosis 16, juvenile (ALS16) [MIM:614373]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:21842496}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neuronopathy, distal hereditary motor, autosomal recessive 2 (HMNR2) [MIM:605726]: A form of distal hereditary motor neuronopathy, a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. HMNR2 is characterized by onset of distal muscle weakness and wasting affecting the lower and upper limbs in the first decade. {ECO:0000269|PubMed:26078401, ECO:0000269|PubMed:27629094}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00321; DB09014; DB00907; DB00514; DB01488; DB00574; DB00502; DB00956; DB00704; DB00540; DB06174; DB00652; DB11186; DB03575; DB05316; DB01708; DB00409; DB01104
Interacts with
Q92847-1; Q99720-1; O00213-2; P17612; P50454; P37173
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Amyotrophic lateral sclerosis; Cell junction; Cell membrane; Cell projection; Cytoplasmic vesicle; Direct protein sequencing; Disease variant; Endoplasmic reticulum; Lipid droplet; Lipid transport; Membrane; Neurodegeneration; Neuropathy; Nucleus; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
A,B,C
Molecular weight

(Da)

20805.3
Length
185
Aromaticity
0.14
Instability index
31.72
Isoelectric point
5.44
Charge

(pH=7)

-6.63
2D Binding mode
Binding energy

(Kcal/mol)

-8.42
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
VFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSRGHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEATAVEWGPNTWMVEYGRGVIPSTLAFALADTVFSTQDFLTLFYTLRSYARGLRLELTTYLFG
Hydrogen bonds contact
Hydrophobic contact
13Histamine H3 receptor (H3R)7F616.18
Target general information
Gen name
HRH3
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Histamine receptor 3; HH3R; GPCR97; G-protein coupled receptor 97; G protein-coupled receptor 97
Protein family
G-protein coupled receptor 1 family
Biochemical class
GPCR rhodopsin
Function
Signals through the inhibition of adenylate cyclase and displays high constitutive activity (spontaneous activity in the absence of agonist). Agonist stimulation of isoform 3 neither modified adenylate cyclase activity nor induced intracellular calcium mobilization. The H3 subclass of histamine receptors could mediate the histamine signals in CNS and peripheral nervous system.
Related diseases
Immunodeficiency 48 (IMD48) [MIM:269840]: A form of severe immunodeficiency characterized by a selective absence of CD8+ T-cells. {ECO:0000269|PubMed:11123350, ECO:0000269|PubMed:11412303, ECO:0000269|PubMed:18509675, ECO:0000269|PubMed:8124727, ECO:0000269|PubMed:8202713}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Autoimmune disease, multisystem, infantile-onset, 2 (ADMIO2) [MIM:617006]: An autosomal recessive, autoimmune disorder characterized by systemic manifestations including blistering skin disease, uncontrollable bullous pemphigoid, inflammatory colitis, autoimmune hypothyroidism, proteinuria and nephrotic syndrome. {ECO:0000269|PubMed:26783323}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01238; DB06698; DB05381; DB17087; DB05080; DB00768; DB11642
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

34321.1
Length
301
Aromaticity
0.16
Instability index
32.22
Isoelectric point
9.63
Charge

(pH=7)

15.11
2D Binding mode
Binding energy

(Kcal/mol)

-8.43
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
RGFSAAWTAVLAALMALLIVATVLGNALVMLAFVADSSLRTQNNFFLLNLAISDFLVGAFCIPLYVPYVLTGRWTFGRGLCKLWLVVDYLLCTSKAFNIVLISYDRFLSVTRAVSYRAQQGDTRRAVRKMLLVWVLAFLLYGPAILSWEYLSGGSSIPEGHCYAEFFYNWYFLITASTLEFFTPFLSVTFFNLSIYLNIQRRTRLRLDGAREAAGRFRLSRDRKVAKSLAVIVSIFGLCWAPYTLLMIIRAACHGHCVPDYWYETSFWLLWANSAVNPVLYPLCHHSFRRAFTKLLCPQKL
Hydrogen bonds contact
Hydrophobic contact
14Leukotriene A-4 hydrolase (LTA4H)3U9W6.16
Target general information
Gen name
LTA4H
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Leukotriene A4 hydrolase; Leukotriene A(4)Leukotriene A-4 hydrolase hydrolase; Leukotriene A(4) hydrolase; LTA4; LTA-H; LTA-4hydrolase; LTA-4 hydrolase
Protein family
Peptidase M1 family
Biochemical class
Ether bond hydrolase
Function
Has also aminopeptidase activity. Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4.
Related diseases
Pigmentary disorder, reticulate, with systemic manifestations, X-linked (PDR) [MIM:301220]: An X-linked recessive disorder characterized by recurrent infections and sterile inflammation in various organs. Diffuse skin hyperpigmentation with a distinctive reticulate pattern is universally evident by early childhood. This is later followed in many patients by hypohidrosis, corneal inflammation and scarring, enterocolitis that resembles inflammatory bowel disease, and recurrent urethral strictures. Melanin and amyloid deposition is present in the dermis. Affected males also have a characteristic facies with frontally upswept hair and flared eyebrows. Female carriers have only restricted pigmentary changes along Blaschko's lines. {ECO:0000269|PubMed:27019227}. The disease is caused by variants affecting the gene represented in this entry. XLPDR is caused by a recurrent intronic mutation that results in missplicing and reduced POLA1 expression. This leads to a decrease in cytosolic RNA:DNA hybrids and constitutive activation of type I interferon responses, but has no effect on cell replication. {ECO:0000269|PubMed:27019227}.; DISEASE: Van Esch-O'Driscoll syndrome (VEODS) [MIM:301030]: An X-linked recessive syndrome characterized by different degrees of intellectual disability, moderate to severe short stature, microcephaly, hypogonadism, and variable congenital malformations. {ECO:0000269|PubMed:31006512}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07102; DB06917; DB07258; DB07094; DB07259; DB02352; DB07292; DB07104; DB06828; DB08466; DB01197; DB05177; DB03366; DB08040; DB06851; DB02062; DB07099; DB07260; DB07196; DB11781; DB03424; DB07237
Interacts with
Q9BSI4
EC number
EC 3.3.2.6
Uniprot keywords
3D-structure; Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; Hydrolase; Leukotriene biosynthesis; Lipid metabolism; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteomics identification; Reference proteome; Zinc
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

68927
Length
608
Aromaticity
0.1
Instability index
38.84
Isoelectric point
5.87
Charge

(pH=7)

-9.86
2D Binding mode
Binding energy

(Kcal/mol)

-8.4
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
IVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD
Hydrogen bonds contact
Hydrophobic contact
15Neuronal acetylcholine receptor subunit alpha-25FJV6.16
Target general information
Gen name
CHRNA2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-2/CHRNA2 sub-subfamily
Biochemical class
NA
Function
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane."
Related diseases
Epilepsy, nocturnal frontal lobe, 4 (ENFL4) [MIM:610353]: An autosomal dominant focal epilepsy characterized by nocturnal seizures associated with fear sensation, tongue movements, and nocturnal wandering, closely resembling nightmares and sleep walking. {ECO:0000269|PubMed:16826524}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Seizures, benign familial infantile, 6 (BFIS6) [MIM:610353]: A form of benign familial infantile epilepsy, a neurologic disorder characterized by afebrile seizures occurring in clusters during the first year of life, without neurologic sequelae. BFIS6 inheritance is autosomal dominant. {ECO:0000269|PubMed:25847220}. The disease may be caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB00732; DB00237; DB00411; DB00565; DB01245; DB00514; DB01135; DB07720; DB00898; DB00472; DB00483; DB08960; DB00657; DB01336; DB00416; DB01226; DB00184; DB01337; DB01338; DB00721; DB00728; DB05740; DB00202; DB01199; DB01339
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Cell membrane; Disease variant; Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Proteomics identification; Receptor; Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix; Transport
Protein physicochemical properties
Chain ID
A,B,C,D,E
Molecular weight

(Da)

120584
Length
1031
Aromaticity
0.14
Instability index
32.21
Isoelectric point
5.62
Charge

(pH=7)

-17.58
2D Binding mode
Binding energy

(Kcal/mol)

-8.4
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
DRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLP
Hydrogen bonds contact
Hydrophobic contact
16Dimethylglycine oxidase1PJ56.16
Target general information
Gen name
dmg
Organism
Arthrobacter globiformis
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
GcvT family
Biochemical class
Oxidoreductase
Function
Dimethylglycine oxidase activity.Nucleotide binding.
Related diseases
Curry-Jones syndrome (CRJS) [MIM:601707]: A multisystem disorder characterized by patchy skin lesions, polysyndactyly, diverse cerebral malformations, unicoronal craniosynostosis, iris colobomas, microphthalmia, and intestinal malrotation with myofibromas or hamartomas. {ECO:0000269|PubMed:24859340, ECO:0000269|PubMed:27236920}. The disease is caused by variants affecting the gene represented in this entry. 8 individuals have been identified with the disease-causing mutation Phe-412 and all were mosaic. The mutation could not be reliably detected in blood, greatest success rates were obtained with affected tissues obtained by invasive procedures. It is thought that the mutation has arisen postzygotically early during embryonic development (PubMed:27236920). This mutation has also been identified in ameloblastoma, medulloblastoma, meningioma, and basal cell carcinoma, and has been reported as the oncogenic driver in some of these tumors (PubMed:24859340). {ECO:0000269|PubMed:24859340, ECO:0000269|PubMed:27236920}.
Drugs

(DrugBank ID)

DB03256; DB03147
Interacts with
NA
EC number
1.5.3.10
Uniprot keywords
3D-structure; Direct protein sequencing; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

45912.2
Length
427
Aromaticity
0.07
Instability index
43.46
Isoelectric point
4.83
Charge

(pH=7)

-20.69
2D Binding mode
Binding energy

(Kcal/mol)

-8.4
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
TPRIVIIGAGIVGTNLADELVTRGWNNITVLDQGPLNMPGGSTSHAPGLVFQTNPSKTMASFAKYTVEKLLSLTEDGVSCFNQVGGLEVATTETRLADLKRKLGYAAAWGIEGRLLSPAECQELYPLLDGENILGGLHVPSDGLASAARAVQLLIKRTESAGVTYRGSTTVTGIEQSGGRVTGVQTADGVIPADIVVSCAGFWGAKIGAMIGMAVPLLPLAHQYVKTTPVPAQQGRNDQPNGARLPILRHQDQDLYYREHGDRYGIGSYAHRPMPVDVDTLGAYAPETVSEHHMPSRLDFTLEDFLPAWEATKQLLPALADSEIEDGFNGIFSFTPDGGPLLGESKELDGFYVAEAVWVTHSAGVAKAMAELLTTGRSETDLGECDITRFEDVQLTPEYVSETSQQNFVEIYDVLHPLQPRLSPRNL
Hydrogen bonds contact
Hydrophobic contact
17P2Y purinoceptor 124PXZ6.15
Target general information
Gen name
P2RY12
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
HORK3
Protein family
G-protein coupled receptor 1 family
Biochemical class
Membrane protein
Function
ADP receptor activity.G-protein coupled adenosine receptor activity.Guanyl-nucleotide exchange factor activity.
Related diseases
Bleeding disorder, platelet-type, 8 (BDPLT8) [MIM:609821]: A condition characterized by mild to moderate mucocutaneous bleeding, and excessive bleeding after surgery or trauma. The defect is due to severe impairment of platelet response to ADP resulting in defective platelet aggregation. {ECO:0000269|PubMed:11196645, ECO:0000269|PubMed:12578987, ECO:0000269|PubMed:25428217}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB06441; DB00758; DB06350; DB01240; DB06209; DB01069; DB05553; DB15163; DB08816; DB00208; DB00374; DB16349
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Blood coagulation; Cell membrane; Disease variant; Disulfide bond; G-protein coupled receptor; Glycoprotein; Hemostasis; Membrane; Phosphoprotein; Proteomics identification; Receptor; Reference proteome; Transducer; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

28830.4
Length
248
Aromaticity
0.17
Instability index
24.19
Isoelectric point
9.39
Charge

(pH=7)

10.55
2D Binding mode
Binding energy

(Kcal/mol)

-8.39
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SLCTRDYKITQVLFPLLYTVLFFVGLITNGLAMRIFFQIRSKSNFIIFLKNTVISDLLMILTFPFKILSDAKLGTGPLRTFVCQVTSVIFYFTMYISISFLGLITIDPKNLLGAKILSVVIWAFMFLLSLPNMILTNRQPRDKNVKKCSFLKSEFGLVWHEIVNYICQVIFWINFLIVVKVFIIIAVFFICFVPFHFARIPYTLSQTRDVFDCTAENTLFYVKESTLWLTSLNACLNPFIYFFLCKSF
Hydrogen bonds contact
Hydrophobic contact
18SEC14-like protein 34UYB6.15
Target general information
Gen name
SEC14L3
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
TAP2
Protein family
NA
Biochemical class
Transport protein
Function
Lipid binding.Transporter activity.
Related diseases
Chondrodysplasia with platyspondyly, distinctive brachydactyly, hydrocephaly, and microphthalmia (CDP-PBHM) [MIM:300863]: A disease characterized by chondrodysplasia, severe platyspondyly, hydrocephaly, and facial features with microphthalmia. Bone abnormalities include a distinctive metaphyseal cupping of the metacarpals, metatarsals, and phalanges. Affected females show a milder phenotype with small stature, sometimes associated with body asymmetry and mild intellectual disability. {ECO:0000269|PubMed:20181727}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB14003; DB14001; DB14002; DB11635; DB11251; DB00163
Interacts with
NA
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Lipid-binding; Proteomics identification; Reference proteome; Transport
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

46148.7
Length
401
Aromaticity
0.1
Instability index
45.19
Isoelectric point
5.79
Charge

(pH=7)

-5.94
2D Binding mode
Binding energy

(Kcal/mol)

-8.39
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
SMSGRVGDLSPKQAETLAKFRENVQDVLPALPNPDDYFLLRWLRARNFDLQKSEALLRKYMEFRKTMDIDHILDWQPPEVIQKYMPGGLCGYDRDGCPVWYDIIGPLDPKGLLFSVTKQDLLKTKMRDCERILHECDLQTERLGKKIETIVMIFDCEGLGLKHFWKPLVEVYQEFFGLLEENYPETLKFMLIVKATKLFPVGYNLMKPFLSEDTRRKIIVLGNNWKEGLLKLISPEELPAQFGGTLTDPDGNPKCLTKINYGGEIPKSMYVRDQVKTQYEHSVQINRGSSHQVEYEILFPGCVLRWQFSSDGADIGFGVFLKTKMGERQRAGEMTEVLPSQRYNAHMVPEDGNLTCSEAGVYVLRFDNTYSFVHAKKVSFTVEVLLPDEGMQKYDKELTPV
Hydrogen bonds contact
Hydrophobic contact
19"Periplasmic trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (Tre37A)"2JG06.14
Target general information
Gen name
treA
Organism
Escherichia coli (strain K12)
Uniprot ID
TTD ID
NA
Synonyms
JW1186;osmA;b1197
Protein family
Glycosyl hydrolase 37 family
Biochemical class
NA
Function
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
Related diseases
SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells. {ECO:0000269|PubMed:2498394, ECO:0000269|PubMed:3093483}.; DISEASE: Thrombocytopenia 6 (THC6) [MIM:616937]: A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC6 is an autosomal dominant form. Affected individuals may also have bone abnormalities and an increased risk for myelofibrosis. {ECO:0000269|PubMed:26936507}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
NA
EC number
3.2.1.28
Uniprot keywords
3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Periplasm; Reference proteome; Signal
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

57508.9
Length
507
Aromaticity
0.11
Instability index
48.32
Isoelectric point
5.48
Charge

(pH=7)

-10.13
2D Binding mode
Binding energy

(Kcal/mol)

-8.38
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMILADYRMQQNQSGFDLRHFVNVNFTLPKYVPPEGQSLREHIDGLWPVLTRSTENTEKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDLNSLMFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQGWYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRANKMATATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQHTYDREKKLVEKYDVSTTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEQPCDNVPATRP
Hydrogen bonds contact
Hydrophobic contact
20Serum albumin (ALB)4L8U6.14
Target general information
Gen name
ALB
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Serum albumin
Protein family
ALB/AFP/VDB family
Biochemical class
NA
Function
Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.
Related diseases
Hyperthyroxinemia, familial dysalbuminemic (FDAH) [MIM:615999]: A disorder characterized by abnormally elevated levels of total serum thyroxine (T4) in euthyroid patients. It is due to abnormal serum albumin that binds T4 with enhanced affinity. {ECO:0000269|PubMed:7852505, ECO:0000269|PubMed:8048949, ECO:0000269|PubMed:9329347, ECO:0000269|PubMed:9589637}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Analbuminemia (ANALBA) [MIM:616000]: A rare autosomal recessive disorder manifested by the presence of a very low amount of circulating serum albumin. Affected individuals manifest mild edema, hypotension, fatigue, and, occasionally, lower body lipodystrophy (mainly in adult females). The most common biochemical finding is hyperlipidemia, with a significant increase in the total and LDL cholesterol concentrations, but normal concentrations of HDL cholesterol and triglycerides. {ECO:0000269|PubMed:8134387}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB08496; DB07517; DB12001; DB05812; DB14973; DB11703; DB01418; DB01614; DB00316; DB00414; DB09347; DB06151; DB00459; DB00787; DB00640; DB00802; DB00346; DB00404; DB00770; DB01370; DB14517; DB14518; DB01118; DB00321; DB01060; DB00415; DB00276; DB06728; DB11901; DB00714; DB04557; DB09229; DB11217; DB00278; DB01238; DB14185; DB09204; DB01169; DB11638; DB09274; DB00126; DB06216; DB01072; DB00335; DB00289; DB01076; DB00995; DB06237; DB07402; DB00993; DB08822; DB08903; DB16703; DB00245; DB01086; DB01053; DB00443; DB14669; DB11967; DB13909; DB01294; DB09223; DB00083; DB09128; DB01222; DB15248; DB00490; DB00237; DB11148; DB06772; DB11751; DB11093; DB11348; DB14481; DB04690; DB01101; DB03600; DB01197; DB01136; DB00456; DB01327; DB14879; DB00274; DB01328; DB01329; DB00493; DB01330; DB00430; DB00438; DB01212; DB06119; DB00567; DB07565; DB08936; DB00878; DB00608; DB00477; DB09093; DB00310; DB00501; DB00568; DB00537; DB00515; DB00349; DB01013; DB00845; DB01242; DB01068; DB00575; DB00758; DB01147; DB00363; DB15534; DB01394; DB00286; DB12483; DB09130; DB01380; DB08865; DB11134; DB06778; DB01176; DB00924; DB00434; DB00847; DB01914; DB06695; DB08912; DB11963; DB04816; DB00080; DB12941; DB01264; DB11943; DB11637; DB01189; DB00304; DB01234; DB14649; DB09213; DB00829; DB01119; DB11397; DB00586; DB00485; DB00266; DB00900; DB00861; DB01396; DB00343; DB08995; DB08930; DB01142; DB00997; DB00254; DB00366; DB04855; DB00476; DB01126; DB01057; DB12243; DB13421; DB00625; DB15444; DB00879; DB00584; DB13874; DB11718; DB00228; DB08899; DB01364; DB00530; DB00303; DB11827; DB12235; DB00783; DB13952; DB13953; DB13954; DB13955; DB13956; DB00655; DB04574; DB00903; DB00977; DB00749; DB00294; DB01276; DB12466; DB04854; DB01039; DB00573; DB00813; DB00950; DB16165; DB01195; DB00687; DB15690; DB00544; DB00472; DB00712; DB08906; DB00983; DB01320; DB06716; DB11796; DB00695; DB15149; DB00743; DB06705; DB01044; DB00317; DB01241; DB12141; DB11978; DB01120; DB01067; DB01016; DB00986; DB13751; DB04539; DB12836; DB11575; DB11359; DB01159; DB14999; DB00070; DB01275; DB00999; DB00774; DB00327; DB09526; DB01611; DB01005; DB00557; DB13014; DB12471; DB09053; DB01050; DB00159; DB01088; DB00619; DB09262; DB00458; DB00808; DB00328; DB07992; DB09564; DB01307; DB05382; DB04711; DB09333; DB00332; DB16200; DB01029; DB00762; DB06636; DB00753; DB00677; DB00951; DB01064; DB00982; DB11757; DB01167; DB08820; DB01587; DB01026; DB01009; DB00598; DB09236; DB00709; DB00555; DB03017; DB01006; DB09237; DB06282; DB01235; DB01137; DB00451; DB00601; DB17083; DB00279; DB01583; DB06655; DB01601; DB09195; DB00678; DB00227; DB09280; DB15935; DB12674; DB00137; DB08932; DB14513; DB01397; DB06796; DB06234; DB00737; DB13959; DB09124; DB00603; DB00784; DB00814; DB01042; DB00454; DB09383; DB00931; DB00333; DB00563; DB00968; DB09241; DB00959; DB06710; DB00264; DB01110; DB00683; DB08893; DB00295; DB01024; DB08231; DB00461; DB00607; DB01183; DB00788; DB00731; DB04861; DB00220; DB11828; DB00238; DB01115; DB11820; DB09079; DB11793; DB12005; DB06713; DB00717; DB00957; DB00540; DB00104; DB00334; DB09074; DB04224; DB00768; DB12455; DB11130; DB04911; DB01083; DB13310; DB01173; DB00526; DB00842; DB00776; DB01062; DB00497; DB06412; DB03585; DB00595; DB15575; DB09073; DB03796; DB13967; DB14582; DB00642; DB00850; DB12978; DB01619; DB03255; DB00946; DB00252; DB01132; DB01621; DB04951; DB00554; DB08860; DB11642; DB01324; DB09087; DB09418; DB06813; DB13514; DB06209; DB01058; DB00860; DB15566; DB14631; DB00635; DB01032; DB01069; DB09348; DB00818; DB00571; DB06480; DB00852; DB00165; DB04216; DB00881; DB00908; DB12874; DB08735; DB00481; DB11853; DB12404; DB00912; DB02709; DB11855; DB01045; DB11753; DB08864; DB08931; DB14840; DB15305; DB00734; DB00503; DB11182; DB00412; DB01098; DB04847; DB06201; DB08877; DB08736; DB00936; DB00938; DB01232; DB11689; DB13928; DB01104; DB01236; DB12965; DB06290; DB00877; DB00815; DB15093; DB00421; DB00649; DB03193; DB06150; DB01581; DB01582; DB00576; DB01015; DB00795; DB00605; DB00391; DB00870; DB00864; DB00675; DB05134; DB09139; DB05521; DB00853; DB14126; DB09299; DB15133; DB00857; DB00342; DB00624; DB13943; DB13944; DB01420; DB13946; DB00759; DB00152; DB11590; DB01622; DB01623; DB09100; DB09070; DB08816; DB01133; DB15171; DB11800; DB01056; DB08895; DB01124; DB00500; DB00273; DB01685; DB00214; DB00755; DB00620; DB00432; DB08814; DB11677; DB00376; DB09069; DB00792; DB00427; DB08867; DB09076; DB12255; DB00313; DB00512; DB05294; DB08881; DB00661; DB15456; DB11641; DB08828; DB00162; DB11739; DB16699; DB00682; DB00943; DB00495; DB00744; DB14533; DB14548; DB00246; DB04828
Interacts with
P02768; P02786; Q8N5Z5; Q6GQQ9-2; Q07869; Q09028; Q86WT6-2; O76024
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Calcium; Cleavage on pair of basic residues; Copper; Direct protein sequencing; Disease variant; Disulfide bond; Glycation; Glycoprotein; Lipid-binding; Metal-binding; Methylation; Phosphoprotein; Proteomics identification; Reference proteome; Repeat; Secreted; Signal; Zinc
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

34028.4
Length
298
Aromaticity
0.09
Instability index
43.45
Isoelectric point
5.49
Charge

(pH=7)

-10.44
2D Binding mode
Binding energy

(Kcal/mol)

-8.37
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
AHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMP
Hydrogen bonds contact
Hydrophobic contact