Structure of PDB 2vct Chain C

Receptor sequence
>2vctC (length=221) Species: 9606 (Homo sapiens) [Search protein sequence]
AEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLM
FQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIAD
LGEMILLLPFTQPEEQDAKLALIQEKTKNRYFPAFEKVLKSHGQDYLVGN
KLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPG
SPRKPPMDEKSLEESRKIFRF
3D structure
PDB2vct Structural Basis for Featuring of Steroid Isomerase Activity in Alpha Class Glutathione Transferases.
ChainC
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y9 R15 R20
Catalytic site (residue number reindexed from 1) Y8 R14 R19
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 ASD C Y9 G14 L108 F111 F222 Y8 G13 L107 F110 F221
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0005515 protein binding
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
GO:0030855 epithelial cell differentiation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vct, PDBe:2vct, PDBj:2vct
PDBsum2vct
PubMed20083122
UniProtP09210|GSTA2_HUMAN Glutathione S-transferase A2 (Gene Name=GSTA2)

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