Structure of PDB 1ml6 Chain B

Receptor sequence
>1ml6B (length=220) Species: 10090 (Mus musculus) [Search protein sequence]
GKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMF
DQVPMVEIDGMKLVQTRAILNYIATKYDLYGKDMKERALIDMYTEGILDL
TEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNR
LTRVDVHLLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKKFLQPGS
QRKPPLDAKQIEEARKVFKF
3D structure
PDB1ml6 Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y308 R314 R319
Catalytic site (residue number reindexed from 1) Y7 R13 R18
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 GBX B D400 R430 D99 R129
BS02 GBX B F309 Q353 V354 Q366 T367 L507 R516 F521 F8 Q52 V53 Q65 T66 L206 R215 F220
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0009617 response to bacterium
GO:0035634 response to stilbenoid
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol

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External links
PDB RCSB:1ml6, PDBe:1ml6, PDBj:1ml6
PDBsum1ml6
PubMed12549910
UniProtP10648|GSTA2_MOUSE Glutathione S-transferase A2 (Gene Name=Gsta2)

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