Structure of PDB 3gst Chain B Binding Site BS01

Receptor Information
>3gst Chain B (length=217) Species: 10117 (Rattus rattus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVE
NQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGD
KVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSS
RYLSTPIFSKLAQWSNK
Ligand information
Ligand IDGPR
InChIInChI=1S/C24H27N3O7S/c25-17(24(33)34)9-10-19(28)27-18(23(32)26-11-20(29)30)12-35-22-16-8-4-2-6-14(16)13-5-1-3-7-15(13)21(22)31/h1-8,17-18,21-22,31H,9-12,25H2,(H,26,32)(H,27,28)(H,29,30)(H,33,34)/t17-,18-,21+,22+/m0/s1
InChIKeyJNNIZILNBMPOAC-MOXQZVSFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc2c(c1)-c3ccccc3C(C2O)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N
OpenEye OEToolkits 1.5.0c1ccc2c(c1)-c3ccccc3[C@H]([C@@H]2O)SC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N
CACTVS 3.341N[C@@H](CCC(=O)N[C@@H](CS[C@H]1[C@H](O)c2ccccc2c3ccccc13)C(=O)NCC(O)=O)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCC(=O)NC(C(=O)NCC(=O)O)CSC3c1ccccc1c2c(cccc2)C3O
CACTVS 3.341N[CH](CCC(=O)N[CH](CS[CH]1[CH](O)c2ccccc2c3ccccc13)C(=O)NCC(O)=O)C(O)=O
FormulaC24 H27 N3 O7 S
Name(9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE
ChEMBL
DrugBankDB01834
ZINCZINC000015685338
PDB chain3gst Chain B Residue 220 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3gst Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Y6 W7 G11 L12 R42 W45 K49 N58 L59 Q71 S72 I111
Binding residue
(residue number reindexed from 1)		Y6 W7 G11 L12 R42 W45 K49 N58 L59 Q71 S72 I111
Annotation score2
Binding affinityMOAD: Ki=0.19uM
PDBbind-CN: -logKd/Ki=6.72,Ki=0.19uM
Enzymatic activity
Catalytic site (original residue number in PDB) Y6 L12 R17
Catalytic site (residue number reindexed from 1) Y6 L12 R17
Enzyme Commision number 2.5.1.18: glutathione transferase.
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0005496 steroid binding
GO:0016151 nickel cation binding
GO:0016740 transferase activity
GO:0019899 enzyme binding
GO:0019901 protein kinase binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043295 glutathione binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0006749 glutathione metabolic process
GO:0007608 sensory perception of smell
GO:0009410 response to xenobiotic stimulus
GO:0010038 response to metal ion
GO:0010288 response to lead ion
GO:0018916 nitrobenzene metabolic process
GO:0042178 xenobiotic catabolic process
GO:0043200 response to amino acid
GO:0045471 response to ethanol
GO:0048678 response to axon injury
GO:0051122 hepoxilin biosynthetic process
GO:0070458 cellular detoxification of nitrogen compound
GO:0071466 cellular response to xenobiotic stimulus
GO:1901687 glutathione derivative biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3gst, PDBe:3gst, PDBj:3gst
PDBsum3gst
PubMed8110735
UniProtP04905|GSTM1_RAT Glutathione S-transferase Mu 1 (Gene Name=Gstm1)

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