Structure of PDB 1f3b Chain B

Receptor sequence
>1f3bB (length=222) Species: 10090 (Mus musculus) [Search protein sequence]
AGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLM
FDQVPMVEIDGMKLAQTRAILNYIATKYDLYGKDMKERALIDMYSEGILD
LTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGN
RLTRVDIHLLEVLLYVEEFDASLLTPFPLLKAFKSRISSLPNVKKFLQPG
SQRKPPMDAKQIQEARKAFKIQ
3D structure
PDB1f3b Residue R216 and catalytic efficiency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y8 R14 R19
Catalytic site (residue number reindexed from 1) Y8 R14 R19
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 GBX B D100 R130 D100 R130
BS02 GBX B Y8 F9 R14 Q53 V54 Q66 T67 R216 I221 Y8 F9 R14 Q53 V54 Q66 T67 R216 I221
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0004601 peroxidase activity
GO:0004769 steroid delta-isomerase activity
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:0009617 response to bacterium
GO:0035634 response to stilbenoid
GO:0098869 cellular oxidant detoxification
GO:1901687 glutathione derivative biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1f3b, PDBe:1f3b, PDBj:1f3b
PDBsum1f3b
PubMed11027134
UniProtP13745|GSTA1_MOUSE Glutathione S-transferase A1 (Gene Name=Gsta1)

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