Structure of PDB 1b4p Chain A Binding Site BS01

Receptor Information
>1b4p Chain A (length=217) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRVDVLE
NQAMDTRLQLAMVCYSPDFERKKPEYLEGLPEKMKLYSEFLGKQPWFAGN
KITYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFVARFEGLKKISDYMKSG
RFLSKPIFAKMAFWNPK
Ligand information
Ligand IDGPS
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-GPHNJDIKSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1ccc2c(c1)-c3ccccc3C(C2O)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N
ACDLabs 12.01O=C(O)C(N)CCC(=O)NC(C(=O)NCC(=O)O)CSC3c1ccccc1c2c(cccc2)C3O
OpenEye OEToolkits 1.7.0c1ccc2c(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 3.370N[CH](CCC(=O)N[CH](CS[CH]1[CH](O)c2ccccc2c3ccccc13)C(=O)NCC(O)=O)C(O)=O
CACTVS 3.370N[C@@H](CCC(=O)N[C@@H](CS[C@@H]1[C@@H](O)c2ccccc2c3ccccc13)C(=O)NCC(O)=O)C(O)=O
FormulaC24 H27 N3 O7 S
NameL-gamma-glutamyl-S-[(9S,10S)-10-hydroxy-9,10-dihydrophenanthren-9-yl]-L-cysteinylglycine
ChEMBL
DrugBankDB04187
ZINCZINC000012501153
PDB chain1b4p Chain A Residue 218 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1b4p The Three-Dimensional Structure of a Glutathione S-Transferease from the Mu Gene Class. Structural Analysis of the Binary Complex of Isoenzyme 3-3 and Glutathione at 2.2-A Resolution
Resolution1.7 Å
Binding residue
(original residue number in PDB)		Y6 W7 V9 G11 R42 W45 K49 N58 L59 Q71 S72 Y115 F208 A209
Binding residue
(residue number reindexed from 1)		Y6 W7 V9 G11 R42 W45 K49 N58 L59 Q71 S72 Y115 F208 A209
Annotation score2
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:0004602 glutathione peroxidase activity
GO:0005102 signaling receptor binding
GO:0005504 fatty acid binding
GO:0016740 transferase activity
GO:0019899 enzyme binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043295 glutathione binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
GO:0007608 sensory perception of smell
GO:0010038 response to metal ion
GO:0010880 regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
GO:0014070 response to organic cyclic compound
GO:0018916 nitrobenzene metabolic process
GO:0033595 response to genistein
GO:0042178 xenobiotic catabolic process
GO:0043651 linoleic acid metabolic process
GO:0051122 hepoxilin biosynthetic process
GO:0070458 cellular detoxification of nitrogen compound
GO:0071313 cellular response to caffeine
GO:0098869 cellular oxidant detoxification
GO:1902168 response to catechin
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016529 sarcoplasmic reticulum
GO:0032991 protein-containing complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1b4p, PDBe:1b4p, PDBj:1b4p
PDBsum1b4p
PubMed
UniProtP08010|GSTM2_RAT Glutathione S-transferase Mu 2 (Gene Name=Gstm2)

[Back to BioLiP]