Structure of PDB 3i6a Chain F

Receptor sequence
>3i6aF (length=217) Species: 9606 (Homo sapiens) [Search protein sequence]
KPKLHYFNGRGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQ
QVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLG
EMIIMLPFCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKL
SRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSP
RKPPPDEIYVRTVYNIF
3D structure
PDB3i6a Structural analysis of a glutathione transferase A1-1 mutant tailored for high catalytic efficiency with toxic alkenals.
ChainF
Resolution1.98 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 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 GSH F D101 R131 D98 R128
BS02 GSH F R15 Q54 V55 Q67 T68 F220 R12 Q51 V52 Q64 T65 F217
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:0005515 protein binding
GO:0016740 transferase activity
GO:0016853 isomerase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0006749 glutathione metabolic process
GO:0006805 xenobiotic metabolic process
GO:0030855 epithelial cell differentiation
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
GO:0070062 extracellular exosome

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Molecular Function
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Cellular Component
External links
PDB RCSB:3i6a, PDBe:3i6a, PDBj:3i6a
PDBsum3i6a
PubMed19618965
UniProtP08263|GSTA1_HUMAN Glutathione S-transferase A1 (Gene Name=GSTA1)

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