Structure of PDB 2vcv Chain E

Receptor sequence
>2vcvE (length=219) Species: 9606 (Homo sapiens) [Search protein sequence]
KPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQ
QVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLN
EMILLLPLCRPEEKDAKIALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKL
SRADISLVELLYYVEELDSSLISNFPLLKALKTRISNLPTVKKFLQPGSP
RKPPADAKALEEARKIFRF
3D structure
PDB2vcv Structural Basis for Featuring of Steroid Isomerase Activity in Alpha Class Glutathione Transferases.
ChainE
Resolution1.8 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) Y6 R12 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 GSH E Y9 R15 R45 Q54 V55 Q67 T68 F220 Y6 R12 R42 Q51 V52 Q64 T65 F217
BS02 ASD E F10 P110 A208 L213 F222 F7 P107 A205 L210 F219
BS03 GSH E D101 R131 D98 R128
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
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:2vcv, PDBe:2vcv, PDBj:2vcv
PDBsum2vcv
PubMed20083122
UniProtQ16772|GSTA3_HUMAN Glutathione S-transferase A3 (Gene Name=GSTA3)

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