Structure of PDB 1gsf Chain A Binding Site BS01

Receptor Information
>1gsf Chain A (length=221) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLM
FQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIAD
LGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGN
KLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEEARKIFRF
Ligand information
Ligand IDEAA
InChIInChI=1S/C13H12Cl2O4/c1-3-7(2)13(18)8-4-5-9(12(15)11(8)14)19-6-10(16)17/h4-5H,2-3,6H2,1H3,(H,16,17)
InChIKeyAVOLMBLBETYQHX-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04Clc1c(C(=O)\C(=C)CC)ccc(OCC(=O)O)c1Cl
CACTVS 3.341CCC(=C)C(=O)c1ccc(OCC(O)=O)c(Cl)c1Cl
OpenEye OEToolkits 1.5.0CCC(=C)C(=O)c1ccc(c(c1Cl)Cl)OCC(=O)O
FormulaC13 H12 Cl2 O4
NameETHACRYNIC ACID
ChEMBLCHEMBL456
DrugBankDB00903
ZINCZINC000000001382
PDB chain1gsf Chain A Residue 223 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1gsf Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		Y9 F10 R15 V55 L107 V111 M208 F220 F222
Binding residue
(residue number reindexed from 1)		Y8 F9 R14 V54 L106 V110 M207 F219 F221
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=5.00,IC50~10uM
BindingDB: IC50=5000nM
Enzymatic activity
Catalytic site (original residue number in PDB) Y9 R15 R20
Catalytic site (residue number reindexed from 1) Y8 R14 R19
Enzyme Commision number 1.11.1.-
2.5.1.18: glutathione transferase.
5.3.3.-
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0004601 peroxidase activity
GO:0004602 glutathione peroxidase activity
GO:0004769 steroid delta-isomerase activity
GO:0005504 fatty acid binding
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0016853 isomerase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
GO:0030855 epithelial cell differentiation
GO:0043651 linoleic acid metabolic process
GO:0098869 cellular oxidant detoxification
GO:1901687 glutathione derivative biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1gsf, PDBe:1gsf, PDBj:1gsf
PDBsum1gsf
PubMed8591048
UniProtP08263|GSTA1_HUMAN Glutathione S-transferase A1 (Gene Name=GSTA1)

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