Structure of PDB 2vqa Chain A

Receptor sequence
>2vqaA (length=356) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence]
WRSLSNVVWGKDLPAFTYAFSKTPLVLYDGGTTKQVGTYNFPVSKGMAGV
YMSLEPGAIRELHWHANAAEWAYVMEGRTRITLTSPEGKVEIADVDKGGL
WYFPRGWGHSIEGIGPDTAKFLLVFNDGTFSEGATFSVTDWLSHTPIAWV
EENLGWTAAQVAQLPKKQVYISSYGPASGPLASATPQGQTAKIEVPHTHN
LLGQQPLVSLGGNELRLASAKEFPGSFNMTGALIHLEPGAMRQLHWHPNA
DEWQYVLDGEMDLTVFASEGKASVSRLQQGDVGYVPKGYGHAIRNSSQKP
LDIVVVFNDGDYQSIDLSTWLASNPSSVLGNTFQISPELTKKLPVQDTIF
SLPTQP
3D structure
PDB2vqa Protein-Folding Location Can Regulate Manganese-Binding Versus Copper- or Zinc-Binding.
ChainA
Resolution2.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R98 H101 H103 E108 H147 E170
Catalytic site (residue number reindexed from 1) R60 H63 H65 E70 H109 E132
Enzyme Commision number ?
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 MN A H101 H103 E108 H147 H63 H65 E70 H109
BS02 MN A H283 H285 E290 H329 H245 H247 E252 H291
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
Biological Process
GO:0033609 oxalate metabolic process
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vqa, PDBe:2vqa, PDBj:2vqa
PDBsum2vqa
PubMed18948958
UniProtP73510

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