Structure of PDB 1c72 Chain D

Receptor sequence
>1c72D (length=217) Species: 9031 (Gallus gallus) [Search protein sequence]
VVTLGYWDIRGLAHAIRLLLEYTETPYQERRYKAGPAPDFDPSDWTNEKE
KLGLDFPNLPYLIDGDVKLTQSNAILRYIARKHNMCGETEVEKQRVDVLE
NHLMDLRMAFARLCYSPDFEKLKPAYLELLPGKLRQLSRFLGSRSWFVGD
KLTFVDFLAYDVLDQQRMFVPDCPELQGNLSQFLQRFEALEKISAYMRSG
RFMKAPIFWYTALWNNK
3D structure
PDB1c72 Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1.
ChainD
Resolution2.8 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 R17
Catalytic site (residue number reindexed from 1) Y6 L12 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 EPY D Y6 W7 L12 P42 W45 N58 L59 Q71 S72 Y6 W7 L12 P42 W45 N58 L59 Q71 S72
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
GO:0042802 identical protein binding
Biological Process
GO:0006629 lipid metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:1c72, PDBe:1c72, PDBj:1c72
PDBsum1c72
PubMed10903867
UniProtP20136|GSTM2_CHICK Glutathione S-transferase 2 (Gene Name=GSTM2)

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