Structure of PDB 4acs Chain B

Receptor sequence
>4acsB (length=217) Species: 9606 (Homo sapiens) [Search protein sequence]
KPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQ
QVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLG
EMIGDLSFSQPEEQDAKLALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKL
SRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSP
RKPPMDEKSLEESRKIF
3D structure
PDB4acs Structure-based redesign of GST A2-2 for enhanced catalytic efficiency with azathioprine.
ChainB
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) 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 B D101 R131 D98 R128
BS02 GSH B R15 Q54 V55 Q67 T68 F220 R12 Q51 V52 Q64 T65 F217
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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Cellular Component
External links
PDB RCSB:4acs, PDBe:4acs, PDBj:4acs
PDBsum4acs
PubMed22444596
UniProtP09210|GSTA2_HUMAN Glutathione S-transferase A2 (Gene Name=GSTA2)

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