Structure of PDB 2gsr Chain A

Receptor sequence
>2gsrA (length=207) Species: 9823 (Sus scrofa) [Search protein sequence]
PPYTITYFPVRGRCEAMRMLLADQDQSWKEEVVTMETWPPLKPSCLFRQL
PKFQDGDLTLYQSNAILRHLGRSFGLYGKDQKEAALVDMVNDGVEDLRCK
YATLIYTNYEAGKEKYVKELPEHLKPFETLLSQNQGGQAFVVGSQISFAD
YNLLDLLRIHQVLNPSCLDAFPLLSAYVARLSARPKIKAFLASPEHVNRP
INGNGKQ
3D structure
PDB2gsr Refined crystal structure of porcine class Pi glutathione S-transferase (pGST P1-1) at 2.1 A resolution.
ChainA
Resolution2.11 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y7 R13 R18
Catalytic site (residue number reindexed from 1) Y7 R13 R18
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 GTS A Y7 F8 R13 W38 K42 Q49 L50 Q62 S63 Y7 F8 R13 W38 K42 Q49 L50 Q62 S63 MOAD: Ki=4uM
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0051122 hepoxilin biosynthetic process
GO:1901687 glutathione derivative biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2gsr, PDBe:2gsr, PDBj:2gsr
PDBsum2gsr
PubMed7932743
UniProtP80031|GSTP1_PIG Glutathione S-transferase P (Gene Name=GSTP1)

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