Structure of PDB 1ev4 Chain D

Receptor sequence
>1ev4D (length=221) Species: 10116 (Rattus norvegicus) [Search protein sequence]
SGKPVLHYFNARGRMECIRFLLAAAGVEFDEKFIQSPEDLEKLKKDGNLM
FDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYSEGILD
LTEMIMQLVICPPDQKEAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGN
KLTRVDIHLLELLLYVEEFDASLLTSFPLLKAFKSRISSLPNVKKFLQPG
SQRKLPMDAKQIEEARKIYKF
3D structure
PDB1ev4 Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y.
ChainD
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.-
2.5.1.18: glutathione transferase.
5.3.3.-
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 D D101 R131 D100 R130
BS02 GTS D R15 K45 Q54 V55 Q67 T68 R14 K44 Q53 V54 Q66 T67
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:0016740 transferase activity
GO:0016853 isomerase activity
GO:0035731 dinitrosyl-iron complex 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:0006805 xenobiotic metabolic process
GO:0009410 response to xenobiotic stimulus
GO:0030855 epithelial cell differentiation
GO:0031667 response to nutrient levels
GO:0042178 xenobiotic catabolic process
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

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Cellular Component
External links
PDB RCSB:1ev4, PDBe:1ev4, PDBj:1ev4
PDBsum1ev4
PubMed11119643
UniProtP00502|GSTA1_RAT Glutathione S-transferase alpha-1 (Gene Name=Gsta1)

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