Structure of PDB 2f3m Chain D

Receptor sequence
>2f3mD (length=218) Species: 9606 (Homo sapiens) [Search protein sequence]
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEK
FKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDIL
ENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAG
NKITFVDFLVYDVLDLHRIFEPKCLDAFPNLKDFISRFEGLEKISAYMKS
SRFLPRPVFSKMAVWGNK
3D structure
PDB2f3m Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a.
ChainD
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y6 L12
Catalytic site (residue number reindexed from 1) Y7 L13
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 GTD D Y6 L12 K49 N58 L59 Q71 S72 Y115 Y7 L13 K50 N59 L60 Q72 S73 Y116
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0019899 enzyme binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043295 glutathione binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006693 prostaglandin metabolic process
GO:0006749 glutathione metabolic process
GO:0018916 nitrobenzene metabolic process
GO:0042178 xenobiotic catabolic process
GO:0051122 hepoxilin biosynthetic process
GO:0070458 cellular detoxification of nitrogen compound
GO:1901687 glutathione derivative biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0045171 intercellular bridge

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Molecular Function
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Cellular Component
External links
PDB RCSB:2f3m, PDBe:2f3m, PDBj:2f3m
PDBsum2f3m
PubMed16548513
UniProtP09488|GSTM1_HUMAN Glutathione S-transferase Mu 1 (Gene Name=GSTM1)

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