Job Results:

Ligand

Structure

Job ID

7bc77a753344ee0c78dc81fd979bf038

Job name

NA

Time

2026-10-07 17:00:49

Rank Target PDB ID AirScore Detail
1"Periplasmic trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (Tre37A)"2JG06.94
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)

-9.47
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMILADYRMQQNQSGFDLRHFVNVNFTLPKYVPPEGQSLREHIDGLWPVLTRSTENTEKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDLNSLMFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQGWYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRANKMATATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQHTYDREKKLVEKYDVSTTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEQPCDNVPATRP
Hydrogen bonds contact
Hydrophobic contact
2Phenylethanolamine N-methyltransferase (PNMT)2G726.92
Target general information
Gen name
PNMT
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
PNMTase; PENT; Noradrenaline N-methyltransferase
Protein family
Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family
Biochemical class
NA
Function
Converts noradrenaline to adrenaline.
Related diseases
A chromosomal aberration involving TRIM24/TIF1 is found in papillary thyroid carcinomas (PTCs). Translocation t(7;10)(q32;q11) with RET. The translocation generates the TRIM24/RET (PTC6) oncogene. {ECO:0000269|PubMed:10439047}.
Drugs

(DrugBank ID)

DB08129; DB08128; DB07739; DB07798; DB07747; DB03468; DB08550; DB03824; DB04273; DB07906; DB07597; DB09571; DB00968; DB08631; DB01752; DB08654
Interacts with
Q9P2G9-2; Q8TBB1
EC number
EC 2.1.1.28
Uniprot keywords
3D-structure; Catecholamine biosynthesis; Direct protein sequencing; Methyltransferase; Phosphoprotein; Proteomics identification; Reference proteome; S-adenosyl-L-methionine; Transferase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

29198.9
Length
264
Aromaticity
0.09
Instability index
54.33
Isoelectric point
5.91
Charge

(pH=7)

-3.69
2D Binding mode
Binding energy

(Kcal/mol)

-9.44
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
APGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKV
Hydrogen bonds contact
Hydrophobic contact
3Caspase-7 (CASP7)1SHJ6.86
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)

-9.35
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
TYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGARCKTLLEKPKLFFIQACRGTEPRYKIPVEADFLFAYSTVRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFKKQIPCVVSMLTKELYFSQVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGARCKTLLEKPKLFFIQACRGPRYKIPVEADFLFAYSTVPGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESKQIPCVVSMLTKELYFSQ
Hydrogen bonds contact
Hydrophobic contact
4Nicotinamide N-methyltransferase2IIP6.85
Target general information
Gen name
NNMT
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
NA
Protein family
Class I-like SAM-binding methyltransferase superfamily, NNMT/PNMT/TEMT family
Biochemical class
Transferase
Function
Nicotinamide N-methyltransferase activity.Pyridine N-methyltransferase activity.
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)

DB00627
Interacts with
NA
EC number
2.1.1.1
Uniprot keywords
3D-structure; Acetylation; Citrullination; Cytoplasm; Direct protein sequencing; Methyltransferase; Proteomics identification; Reference proteome; S-adenosyl-L-methionine; Transferase
Protein physicochemical properties
Chain ID
A,B,C,D
Molecular weight

(Da)

27886.8
Length
251
Aromaticity
0.1
Instability index
40.66
Isoelectric point
5.23
Charge

(pH=7)

-5.11
2D Binding mode
Binding energy

(Kcal/mol)

-9.35
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GFTSKDTYLSHFNPRDYLEKYYSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKAAPAAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKL
Hydrogen bonds contact
Hydrophobic contact
5Folate receptor alpha (FOLR1)4LRH6.83
Target general information
Gen name
FOLR1
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Ovarian tumorassociated antigen MOv18; KB cells FBP; Folate receptor, adult; Folate receptor 1; FRalpha; FOLR1; Adult folatebinding protein
Protein family
Folate receptor family
Biochemical class
Folate receptor
Function
Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pHafter receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release. Required for normal embryonic development and normal cell proliferation.
Related diseases
Neurodegeneration due to cerebral folate transport deficiency (NCFTD) [MIM:613068]: An autosomal recessive neurodegenerative disorder resulting from brain-specific folate deficiency early in life. Onset is apparent in late infancy with severe developmental regression, movement disturbances, epilepsy and leukodystrophy. {ECO:0000269|PubMed:19732866}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB05595; DB00158; DB00563; DB12489; DB15413; DB05168
Interacts with
Q8N357
EC number
NA
Uniprot keywords
3D-structure; Cell membrane; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Endosome; Folate-binding; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Neurodegeneration; Proteomics identification; Receptor; Reference proteome; Secreted; Signal; Transport
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

24216
Length
207
Aromaticity
0.13
Instability index
49.36
Isoelectric point
8.14
Charge

(pH=7)

3.41
2D Binding mode
Binding energy

(Kcal/mol)

-9.31
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
RTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTVLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMSGT
Hydrogen bonds contact
Hydrophobic contact
6Protein cereblon (CRBN)5FQD6.81
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)

-9.29
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
EFIVGGKYKLNITNGEEVAVINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEIVKVKAIGRQRFKVLEQQAKVQILPECVLAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPD
Hydrogen bonds contact
Hydrophobic contact
7Bacterial Oxoacyl-[acyl-carrier-protein] synthase II (Bact fabF)2GFX6.81
Target general information
Gen name
Bact fabF
Organism
Escherichia coli (strain K12)
Uniprot ID
TTD ID
Synonyms
KASB; KAS II; KAS 2; FabF; Condensing enzyme FabF; Beta-ketoacyl-acyl carrier protein synthase B; Beta-ketoacyl-ACP synthase II; Beta-ketoacyl-ACP synthase 2; 3-oxoacyl-[acyl-carrier-protein] synthase
Protein family
Thiolase-like superfamily, Beta-ketoacyl-ACP synthases family
Biochemical class
Acyltransferase
Function
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
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)

DB08366; DB01034; DB03017; DB08407
Interacts with
P0A6Y8
EC number
EC 2.3.1.179
Uniprot keywords
3D-structure; Acyltransferase; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

42852
Length
411
Aromaticity
0.06
Instability index
31.41
Isoelectric point
5.72
Charge

(pH=7)

-7.34
2D Binding mode
Binding energy

(Kcal/mol)

-9.29
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
KRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATAQTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
Hydrogen bonds contact
Hydrophobic contact
8Monoglyceride lipase (MAGL)3PE66.80
Target general information
Gen name
MGLL
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Monoacylglycerol lipase; MGL; Lysophospholipaselike; Lysophospholipase-like; Lysophospholipase homolog; HUK5; HU-K5
Protein family
AB hydrolase superfamily, Monoacylglycerol lipase family
Biochemical class
Carboxylic ester hydrolase
Function
Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain. Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth. Converts monoacylglycerides to free fatty acids and glycerol.
Related diseases
Systemic lupus erythematosus 9 (SLEB9) [MIM:610927]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. {ECO:0000269|PubMed:17360460}. Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Immunodeficiency, common variable, 7 (CVID7) [MIM:614699]: A primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low. {ECO:0000269|PubMed:22035880}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
P07550; P37235
EC number
EC 3.1.1.23
Uniprot keywords
3D-structure; Alternative splicing; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase; Lipid biosynthesis; Lipid degradation; Lipid metabolism; Membrane; Nitration; Phosphoprotein; Proteomics identification; Reference proteome; Serine esterase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

31808.4
Length
289
Aromaticity
0.08
Instability index
29.7
Isoelectric point
6.73
Charge

(pH=7)

-0.91
2D Binding mode
Binding energy

(Kcal/mol)

-9.28
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PRRTPQSIPYQDLPHLVNADGQYLFCRYWAPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNSVLPNLSSGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTA
Hydrogen bonds contact
Hydrophobic contact
9Zinc finger protein Helios (IKZF2)7LPS6.80
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)

-9.27
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
INFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDGERPFHCNQCGASFTQKGNLLRHIKLHSG
Hydrogen bonds contact
Hydrophobic contact
10Thyroid hormone receptor beta (THRB)1N466.79
Target general information
Gen name
THRB
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
c-erbA-beta; c-erbA-2; THR1; Nuclear receptor subfamily 1 group A member 2; NR1A2; ERBA2
Protein family
Nuclear hormone receptor family, NR1 subfamily
Biochemical class
Nuclear hormone receptor
Function
High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Nuclear hormone receptor that can act as a repressor or activator of transcription.
Related diseases
Thyroid hormone resistance, generalized, autosomal dominant (GRTHD) [MIM:188570]: An autosomal dominant disease characterized by high levels of circulating thyroid hormones (T3-T4), goiter, abnormal mental functions, increased susceptibility to infections, abnormal growth and bone maturation, tachycardia and deafness. Affected individuals may also have attention deficit-hyperactivity disorders (ADHD) and language difficulties. Patients have normal or slightly elevated thyroid stimulating hormone (TSH). {ECO:0000269|PubMed:10660344, ECO:0000269|PubMed:12511610, ECO:0000269|PubMed:12554782, ECO:0000269|PubMed:1314846, ECO:0000269|PubMed:1324420, ECO:0000269|PubMed:1563081, ECO:0000269|PubMed:1587388, ECO:0000269|PubMed:1619012, ECO:0000269|PubMed:1661299, ECO:0000269|PubMed:16804041, ECO:0000269|PubMed:1846005, ECO:0000269|PubMed:19268523, ECO:0000269|PubMed:2153155, ECO:0000269|PubMed:2510172, ECO:0000269|PubMed:7833659, ECO:0000269|PubMed:8175986, ECO:0000269|PubMed:8514853, ECO:0000269|PubMed:8664910, ECO:0000269|PubMed:8889584}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thyroid hormone resistance, generalized, autosomal recessive (GRTHR) [MIM:274300]: An autosomal recessive disorder characterized by goiter, clinical euthyroidism, end-organ unresponsiveness to thyroid hormone, abnormal growth and bone maturation, and deafness. Patients also have high levels of circulating thyroid hormones, with elevated thyroid stimulating hormone. {ECO:0000269|PubMed:1653889}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Selective pituitary thyroid hormone resistance (PRTH) [MIM:145650]: Variant form of thyroid hormone resistance and is characterized by clinical hyperthyroidism, with elevated free thyroid hormones, but inappropriately normal serum TSH. Unlike GRTH, where the syndrome usually segregates with a dominant allele, the mode of inheritance in PRTH has not been established. {ECO:0000269|PubMed:7528740, ECO:0000269|PubMed:8381821}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB08085; DB03181; DB02106; DB01118; DB00509; DB05035; DB03788; DB03176; DB00451; DB00279; DB01583; DB05192; DB07425; DB09100; DB03604
Interacts with
Q60974; Q9Y618
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Deafness; Disease variant; DNA-binding; Metal-binding; Nucleus; Proteomics identification; Receptor; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

27235.4
Length
239
Aromaticity
0.09
Instability index
43.29
Isoelectric point
5.42
Charge

(pH=7)

-8.55
2D Binding mode
Binding energy

(Kcal/mol)

-9.27
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
KPEPTDEEWELIKTVTEAHVATNAQWKQKRKFLPEDIGQAKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
Hydrogen bonds contact
Hydrophobic contact
11Plasmodium Dihydroorotate dehydrogenase (Malaria DHOdehase)1TV56.79
Target general information
Gen name
Malaria DHOdehase
Organism
Plasmodium falciparum (isolate 3D7)
Uniprot ID
TTD ID
Synonyms
PFF0160c; Mitochondrially bound dihydroorotate-ubiqui oxidoreductase; Dihydroorotate oxidase of Plasmodium falciparum; Dihydroorotate dehydrogenase of Plasmodium falciparum; DHOdehase of Plasmodium fa
Protein family
Dihydroorotate dehydrogenase family, Type 2 subfamily
Biochemical class
CH-CH donor oxidoreductase
Function
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Related diseases
Combined oxidative phosphorylation deficiency 33 (COXPD33) [MIM:617713]: An autosomal recessive disorder caused by multiple mitochondrial respiratory chain defects and impaired mitochondrial energy metabolism. Clinical manifestations are highly variable. Affected infants present with cardiomyopathy accompanied by multisystemic features involving liver, kidney, and brain. Death in infancy is observed in some patients. Children and adults present with myopathy and progressive external ophthalmoplegia. {ECO:0000269|PubMed:28942965}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01117
Interacts with
NA
EC number
EC 1.3.5.2
Uniprot keywords
3D-structure; Flavoprotein; FMN; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Pyrimidine biosynthesis; Reference proteome; Transit peptide; Transmembrane; Transmembrane helix
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

41846.8
Length
371
Aromaticity
0.1
Instability index
37.25
Isoelectric point
8.21
Charge

(pH=7)

3.13
2D Binding mode
Binding energy

(Kcal/mol)

-9.27
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
FESYNPEFFLYDIFLKFCLKYIDGEICHDLFLLLGKYNILPYDTSNDSIYACTNIKHLDFINPFGVAAGFDKNGVCIDSILKLGFSFIEIGTITPRGQTGNAKPRIFRDVESRSIINSCGFNNMGCDKVTENLILFRKRQEEDKLLSKHIVGVSIGKNKDTVNIVDDLKYCINKIGRYADYIAINVSSPNTPGLRDNQEAGKLKNIILSVKEEIDNLEFLWFNTTKKKPLVFVKLAPDLNQEQKKEIADVLLETNIDGMIISNTTTQINDIKSFENKKGGVSGAKLKDISTKFICEMYNYTNKQIPIIASGGIFSGLDALEKIEAGASVCQLYSCLVFNGMKSAVQIKRELNHLLYQRGYYNLKEAIGRKH
Hydrogen bonds contact
Hydrophobic contact
12Retinoic acid receptor alpha (RARA)3KMR6.78
Target general information
Gen name
RARA
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
RAR-alpha; RAR alpha; Nuclear receptor subfamily 1 group B member 1; NR1B1
Protein family
Nuclear hormone receptor family, NR1 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 RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. Receptor for retinoic acid.
Related diseases
Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled-coil domain functions in blocking RA-mediated transactivation and cell differentiation. {ECO:0000269|PubMed:12691149, ECO:0000269|PubMed:8302850, ECO:0000269|PubMed:8562957}.
Drugs

(DrugBank ID)

DB00459; DB00210; DB00523; DB00926; DB00982; DB05785; DB04942; DB00799; DB00755; DB12808
Interacts with
O43707-1; O15296; Q15699; Q96RK4; O95273; P51946; Q15910; P50148; Q9UKP3; Q96EZ8; Q15648; Q71SY5; Q15788; Q9Y6Q9; O75376; Q9Y618; Q16236; P13056-2; P48552; Q9UPP1-2; Q9H8W4; P37231; P78527; P19793; P28702; P28702-3; P48443; Q96EB6; P63165; Q8WW24; Q2M1K9; Q91XC0; P59598; Q14457; P48552; Q96CV9; P28702; P48443; Q8WW24
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Chromosomal rearrangement; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; Proto-oncogene; Receptor; Reference proteome; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

27724.1
Length
244
Aromaticity
0.05
Instability index
50.8
Isoelectric point
5.82
Charge

(pH=7)

-3.61
2D Binding mode
Binding energy

(Kcal/mol)

-9.25
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
PEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDRVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLEHKILHRLLQE
Hydrogen bonds contact
Hydrophobic contact
13Tyrosine-protein kinase Kit (KIT)1T466.75
Target general information
Gen name
KIT
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog; p145 c-kit; Proto-oncogene tyrosine-protein kinase Kit; Proto-oncogene c-Kit; Piebald trait protein; PBT; Mast/stem cell growth factor re
Protein family
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
Biochemical class
Kinase
Function
In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1. Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis.
Related diseases
Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes. {ECO:0000269|PubMed:11074500, ECO:0000269|PubMed:1370874, ECO:0000269|PubMed:1376329, ECO:0000269|PubMed:1717985, ECO:0000269|PubMed:7687267, ECO:0000269|PubMed:8680409, ECO:0000269|PubMed:9450866, ECO:0000269|PubMed:9699740}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Gastrointestinal stromal tumor (GIST) [MIM:606764]: Common mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery. {ECO:0000269|PubMed:11505412, ECO:0000269|PubMed:15824741, ECO:0000269|PubMed:9438854, ECO:0000269|PubMed:9697690}. The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. The gene represented in this entry is involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of KIT are detected in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the kinase domain can result in a constitutively activated kinase.; DISEASE: Mastocytosis, cutaneous (MASTC) [MIM:154800]: A form of mastocytosis, a heterogeneous group of disorders associated with abnormal proliferation and accumulation of mast cells in various tissues, especially in the skin and hematopoietic organs. MASTC is an autosomal dominant form characterized by macules, papules, nodules, or diffuse infiltration of the skin, often associated with localized hyperpigmentation. Gentle rubbing of the lesions induces histamine release from mechanically activated mast cells, causing local wheals, erythema, and often pruritus, a phenomenon termed Darier sign. {ECO:0000269|PubMed:15173254, ECO:0000269|PubMed:19865100, ECO:0000269|PubMed:21689725, ECO:0000269|PubMed:24289326, ECO:0000269|PubMed:9990072}. The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mastocytosis, systemic (MASTSYS) [MIM:154800]: A severe form of mastocytosis characterized by abnormal proliferation and accumulation of mast cells in several organs, resulting in a systemic disease that may affect bone, gastrointestinal tract, lymphatics, spleen, and liver. In some cases, it is associated with a clonal hematologic non-mast-cell lineage disease, such as a myelodysplastic or myeloproliferative disorder. It can also lead to mast cell leukemia, which carries a high risk of mortality. {ECO:0000269|PubMed:9990072}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB12742; DB09103; DB15233; DB01254; DB12147; DB12010; DB00619; DB09078; DB06080; DB06595; DB04868; DB05913; DB06589; DB12978; DB01962; DB08901; DB08896; DB14840; DB00398; DB01268; DB11800; DB05146
Interacts with
P00519; P42684; O75815; P51451; Q8WV28; P46108; P07332; P09769; O75791; P62993; Q14451; P08631; Q96JZ2; P21583; P06239; P07948; P16333; O43639; P27986; O00459; Q92569; P19174; P16885; Q13882; Q06124; Q92729; P20936; Q9UQQ2; O14796; Q9NP31; Q8N5H7; P78314; Q15464; P29353; P98077; Q92529; Q9H6Q3; O14508; O14543; O14544; P12931; Q9ULZ2; Q9HBL0; Q63HR2; Q68CZ2; P42681; P07947; P43403; Q8VBX6; P35235
EC number
EC 2.7.10.1
Uniprot keywords
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Magnesium; Membrane; Metal-binding; 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)

33575.6
Length
297
Aromaticity
0.11
Instability index
45.37
Isoelectric point
8.37
Charge

(pH=7)

3.24
2D Binding mode
Binding energy

(Kcal/mol)

-9.21
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFLALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTN
Hydrogen bonds contact
Hydrophobic contact
14Programmed cell death 1 ligand 1 (PD-L1)5J896.75
Target general information
Gen name
CD274
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
hPD-L1; Programmed death ligand 1; PDL1; PDCD1LG1; PDCD1L1; PDCD1 ligand 1; B7H1; B7-H1; B7 homolog 1
Protein family
Immunoglobulin superfamily, BTN/MOG family
Biochemical class
Immunoglobulin
Function
As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response. Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10). Plays a critical role in induction and maintenance of immune tolerance to self.
Related diseases
Truncation of the 3'-untranslated (3'-UTR) region of CD274 transcripts leads to elevated expression of CD274 in multiple cancers including T-cell leukemia, diffuse large B-cell lymphoma and stomach adenocarcinoma (PubMed:27281199). Disruption of 3'-UTR region is caused by structural variants that stabilize CD274 transcripts, leading to overexpression (PubMed:27281199). Increased expression in tumors promotes immune evasion and tumor cell growth by allowing malignant cells to escape destruction by the immune system (PubMed:27281199). {ECO:0000269|PubMed:27281199}.
Drugs

(DrugBank ID)

DB15773; DB11595; DB15771; DB11945; DB15772; DB14776; DB15770; DB11714; DB15769; DB09035; DB09037; DB00203; DB00313
Interacts with
P33681; Q8IZR5; Q9NX76; Q15116; Q15116
EC number
NA
Uniprot keywords
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond; Endosome; Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Nucleus; Proteomics identification; Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane; Transmembrane helix; Ubl conjugation
Protein physicochemical properties
Chain ID
C,D
Molecular weight

(Da)

28335.2
Length
249
Aromaticity
0.1
Instability index
35.39
Isoelectric point
6.15
Charge

(pH=7)

-3.43
2D Binding mode
Binding energy

(Kcal/mol)

-9.2
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
AFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYAAALEHHHAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYAAALEHH
Hydrogen bonds contact
Hydrophobic contact
15Thyroid hormone receptor alpha (THRA)3ILZ6.74
Target general information
Gen name
THRA
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
V-erbA-related protein 7; THRA2; THRA1; Nuclear receptor subfamily 1 group A member 1; NR1A1; ERBA1; EAR7; EAR-7; C-erbA-alpha; C-erbA-1
Protein family
Nuclear hormone receptor family, NR1 subfamily
Biochemical class
Nuclear hormone receptor
Function
High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Isoform Alpha-1: Nuclear hormone receptor that can act as a repressor or activator of transcription.
Related diseases
Hypothyroidism, congenital, non-goitrous, 6 (CHNG6) [MIM:614450]: A disease characterized by growth retardation, developmental retardation, skeletal dysplasia, borderline low thyroxine levels and high triiodothyronine levels. There is differential sensitivity to thyroid hormone action, with retention of hormone responsiveness in the hypothalamic pituitary axis and liver but skeletal, gastrointestinal, and myocardial resistance. {ECO:0000269|PubMed:22168587, ECO:0000269|PubMed:24969835, ECO:0000269|PubMed:25670821, ECO:0000269|PubMed:26037512}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01118; DB00509; DB04855; DB05035; DB03176; DB00451; DB00279; DB01583; DB05235; DB09100
Interacts with
Q9Y2J4; Q9Y2J4-4; O95971; Q8TAP6; Q96JM7; Q15648; Q6FHY5; P31321; Q96A49; O75410-7; Q9JLI4
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Congenital hypothyroidism; Cytoplasm; Disease variant; DNA-binding; Metal-binding; Nucleus; Proteomics identification; Receptor; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

29910.1
Length
267
Aromaticity
0.07
Instability index
52.75
Isoelectric point
5.31
Charge

(pH=7)

-11.32
2D Binding mode
Binding energy

(Kcal/mol)

-9.2
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GSHMEEMIRSLQQRPEPTPEEWDLIHIATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPXEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQAVLLMSTDRSGLLXVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKVTDLRMIGAXHASRFLHMKVEXPTELFPPLFLEVFEDQEV
Hydrogen bonds contact
Hydrophobic contact
16Nitric-oxide synthase inducible (NOS2)3E7G6.74
Target general information
Gen name
NOS2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
iNOS; Peptidyl-cysteine S-nitrosylase NOS2; Nitric oxide synthase, inducible; NOS2A; NOS type II; Inducible NOS; Inducible NO synthase; Hepatocyte NOS; HEP-NOS
Protein family
NOS family
Biochemical class
Paired donor oxygen oxidoreductase
Function
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8.
Related diseases
Cerebellar ataxia, impaired intellectual development, and dysequilibrium syndrome 3 (CAMRQ3) [MIM:613227]: An autosomal recessive, congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and intellectual disability. {ECO:0000269|PubMed:19461874}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB07003; DB07007; DB07011; DB07405; DB08750; DB01997; DB07029; DB07008; DB08214; DB07002; DB01835; DB06879; DB04534; DB03100; DB02207; DB00125; DB00155; DB01234; DB14649; DB11327; DB00997; DB07306; DB07388; DB05252; DB01381; DB03366; DB05214; DB04400; DB09237; DB00244; DB01110; DB01017; DB03144; DB01686; DB03449; DB06916; DB07318; DB07389; DB02044; DB02644; DB05383; DB02234; DB03953; DB02462; DB08814
Interacts with
P04406
EC number
EC 1.14.13.39
Uniprot keywords
3D-structure; Alternative splicing; Calcium; Calmodulin-binding; Cytoplasm; FAD; Flavoprotein; FMN; Heme; Iron; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Proteomics identification; Reference proteome; Ubl conjugation; Zinc
Protein physicochemical properties
Chain ID
A,B,C,D
Molecular weight

(Da)

48633
Length
421
Aromaticity
0.12
Instability index
46.5
Isoelectric point
6.75
Charge

(pH=7)

-1.04
2D Binding mode
Binding energy

(Kcal/mol)

-9.19
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
RHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVWQD
Hydrogen bonds contact
Hydrophobic contact
17SEC14-like protein 44TLG6.73
Target general information
Gen name
SEC14L4
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
NA
Synonyms
TAP3
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; DB11635; DB11251; DB00163
Interacts with
Q96LC9; O43186; P78358; Q9NYQ3; Q0VD86; Q15323; O76011; P50221; Q6FHY5; Q02548; P26367; Q9H8W4; Q04864; Q04864-2; Q9UHV2; P15884; P15884-3; Q96N21; Q9BYV2; Q8N6Y0; Q9H0C1
EC number
NA
Uniprot keywords
3D-structure; Alternative splicing; Lipid-binding; Proteomics identification; Reference proteome; Transport
Protein physicochemical properties
Chain ID
A,B
Molecular weight

(Da)

23947.6
Length
210
Aromaticity
0.1
Instability index
50.84
Isoelectric point
5.55
Charge

(pH=7)

-3.11
2D Binding mode
Binding energy

(Kcal/mol)

-9.18
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
VTWQPPEVIQLYDSGGLCGYDYEGCPVYFNIIGSLDPKGLLLSASKQDMIRKRIKVCELLLHECELQTQKLGRKIEMALMVFDMEGLSLKHLWKPAVEVYQQFFSILEANYPETLKNLIVIRAPKLFPVAFNLVKSFMSEETRRKIVILGDNWKQELTKFISPDQLPVEFGGTMTDPDGNPKCLTKINYGGEVPKSYYPDKASEETLQSM
Hydrogen bonds contact
Hydrophobic contact
18Tankyrase-2 (TNKS-2)3U9H6.73
Target general information
Gen name
TNKS2
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Tankyrase-related protein; Tankyrase-like protein; Tankyrase II; TRF1-interacting ankyrin-related ADP-ribose polymerase 2; TNKL; TANK2; Protein poly-ADP-ribosyltransferase tankyrase-2; Poly [ADP-ribos
Protein family
ARTD/PARP family
Biochemical class
Glycosyltransferases
Function
Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. Stimulates 26S proteasome activity. Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking.
Related diseases
Intellectual developmental disorder with macrocephaly, seizures, and speech delay (IDDMSSD) [MIM:618158]: An autosomal dominant neurodevelopmental disorder characterized by impaired intellectual development, poor speech, postnatal macrocephaly, and seizures. {ECO:0000269|PubMed:30290153}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
O15084; Q7Z6K5-1; O15169; Q9NWV8; P11274; Q13698; Q9NRI5; Q6V0I7; Q9NWT6; P14652; Q9UIQ6; Q14980; Q9BZL4; Q92698; P78314; O43815; P54274; Q9C0C2; Q9UHP3; Q06649
EC number
EC 2.4.2.30
Uniprot keywords
3D-structure; ADP-ribosylation; ANK repeat; Chromosome; Cytoplasm; Glycosyltransferase; Golgi apparatus; Hydroxylation; Membrane; Metal-binding; NAD; Nucleotidyltransferase; Nucleus; Proteomics identification; Reference proteome; Repeat; Telomere; Transferase; Ubl conjugation; Wnt signaling pathway; Zinc
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

23695.5
Length
208
Aromaticity
0.11
Instability index
47.61
Isoelectric point
8.28
Charge

(pH=7)

2.88
2D Binding mode
Binding energy

(Kcal/mol)

-9.18
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
GTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRPE
Hydrogen bonds contact
Hydrophobic contact
19WNK lysine-deficient protein kinase 3 (WNK3)5O2B6.72
Target general information
Gen name
WNK3
Organism
Homo sapiens (Human)
Uniprot ID
TTD ID
Synonyms
Serine/threonine-protein kinase WNK3; Protein kinase with no lysine 3; Protein kinase lysine-deficient 3; KIAA1566
Protein family
Protein kinase superfamily, Ser/Thr protein kinase family, WNK subfamily
Biochemical class
NA
Function
Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Phosphorylates WNK4. Regulates the phosphorylation of SLC12A1 and SLC12A2. Increases Ca(2+) influx mediated by TRPV5 and TRPV6 by enhancing their membrane expression level via a kinase-dependent pathway. Inhibits the activity of KCNJ1 by decreasing its expression at the cell membrane in a non-catalytic manner.
Related diseases
Prieto syndrome (PRS) [MIM:309610]: An X-linked recessive disorder characterized by impaired intellectual development, developmental delay, autism spectrum disorder, variable epilepsy, craniofacial dysmorphism, and structural brain abnormalities including polymicrogyria and cerebral atrophy. {ECO:0000269|PubMed:35678782}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

NA
Interacts with
P42574; P52954; Q04864-2
EC number
EC 2.7.11.1
Uniprot keywords
3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Disease variant; Intellectual disability; Kinase; Nucleotide-binding; Phosphoprotein; Proteomics identification; Reference proteome; Serine/threonine-protein kinase; Transferase; Ubl conjugation
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

30818.4
Length
269
Aromaticity
0.1
Instability index
41.03
Isoelectric point
6.27
Charge

(pH=7)

-2.07
2D Binding mode
Binding energy

(Kcal/mol)

-9.17
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
MEAEMKAVATSPSGRFLKFDIELGRGAFKTVYKGLDTETWVEVAWCELQLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESIKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLMIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIRDLLNHAFFAEDTGLRVE
Hydrogen bonds contact
Hydrophobic contact
20Cyclopropane mycolic acid synthase MmaA21TPY6.72
Target general information
Gen name
mmaA2
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Uniprot ID
TTD ID
NA
Synonyms
Rv0644c;mma2
Protein family
CFA/CMAS family
Biochemical class
Transferase
Function
Cyclopropane-fatty-acyl-phospholipid synthase activity.Methyltransferase activity.
Related diseases
Oocyte/zygote/embryo maturation arrest 16 (OZEMA16) [MIM:617234]: A rare cause of female primary infertility. In affected women, ovulation and fertilization proceed normally but embryos are arrested at early stages of development. Inheritance is autosomal recessive. {ECO:0000269|PubMed:27545678}. The disease is caused by variants affecting the gene represented in this entry.
Drugs

(DrugBank ID)

DB01718; DB01752
Interacts with
NA
EC number
2.1.1.79
Uniprot keywords
3D-structure; Acetylation; Lipid biosynthesis; Lipid metabolism; Methyltransferase; Reference proteome; S-adenosyl-L-methionine; Transferase
Protein physicochemical properties
Chain ID
A
Molecular weight

(Da)

32493.6
Length
285
Aromaticity
0.1
Instability index
43.61
Isoelectric point
5.53
Charge

(pH=7)

-10.17
2D Binding mode
Binding energy

(Kcal/mol)

-9.16
Molscript Map
Pymol Map
Ligplot Map
3D Binding mode
Sequence
NDLTPHFEDVQAHYDLSDDFFRLFLDPTQTYSCAHFEREDMTLEEAQIAKIDLALGKLGLQPGMTLLDIGCGWGATMRRAIAQYDVNVVGLTLSKNQAAHVQKSFDEMDTPRDRRVLLAGWEQFNEPVDRIVSIGAFEHFGHDRHADFFARAHKILPPDGVLLLHTITGLTRQQMVDHGLPLTLWLARFLKFIATEIFPGGQPPTIEMVEEQSAKTGFTLTRRQSLQPHYARTLDLWAEALQEHKSEAIAIQSEEVYERYMKYLTGCAKLFRVGYIDVNQFTLAK
Hydrogen bonds contact
Hydrophobic contact