Structure of PDB 2pvq Chain A

Receptor sequence
>2pvqA (length=201) Species: 529 (Brucella anthropi) [Search protein sequence]
MKLYYKVGAASLAPHIILSEAGLPYELEAVDLKAKKTADGGDYFAVNPRG
AVPALEVKPGTVITQNAAILQYIGDHSDVAAFKPAYGSIERARLQEALGF
CSDLHAAFSGLFAPNLSEEARAGVIANINRRLGQLEAMLSDKNAYWLGDD
FTQPDAYASVIIGWGVGQKLDLSAYPKALKLRERVLARPNVQKAFKEEGL
N
3D structure
PDB2pvq Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site.
ChainA
Resolution1.803 Å
3D
structure
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Enzymatic activity
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 GSH A V7 G8 A9 A10 H105 S109 F112 W164 V7 G8 A9 A10 H105 S109 F112 W164
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016740 transferase activity
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:2pvq, PDBe:2pvq, PDBj:2pvq
PDBsum2pvq
PubMed18076047
UniProtP81065|GST_BRUAN Glutathione S-transferase (Gene Name=gst)

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