Structure of PDB 3gst Chain B

Receptor sequence
>3gstB (length=217) Species: 10117 (Rattus rattus) [Search protein sequence]
PMILGYWNVRGLTHPIRLLLEYTDSSYEEKRYAMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGSRKITQSNAIMRYLARKHHLCGETEEERIRADIVE
NQVMDNRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGD
KVTYVDFLAYDILDQYHIFEPKCLDAFPNLKDFLARFEGLKKISAYMKSS
RYLSTPIFSKLAQWSNK
3D structure
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.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GPR B Y6 W7 G11 L12 R42 W45 K49 N58 L59 Q71 S72 I111 Y6 W7 G11 L12 R42 W45 K49 N58 L59 Q71 S72 I111 MOAD: Ki=0.19uM
PDBbind-CN: -logKd/Ki=6.72,Ki=0.19uM
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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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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