Structure of PDB 2f7v Chain A Binding Site BS01

Receptor Information
>2f7v Chain A (length=360) Species: 339 (Xanthomonas campestris) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMTDLLASTLEHLETLVSFDTRNPPRAIAAEGGIFDYLRAQLPGFQVEVI
DHGDGAVSLYAVRGTPKYLFNVHLDTVPDSPHWSADPHVMRRTEDRVIGL
GVCDIKGAAAALVAAANAGDGDAAFLFSSDEEANDPRCIAAFLARGLPYD
AVLVAEPTMSEAVLAHRGISSVLMRFAGRAGDPAASALHQAMRWGGKALD
HVESLAHARFGGLTGLRFNIGRVDGGIKANMIAPAAELRFGFRPLPSMDV
DGLLATFAGFADPAAAHFEETFRGPSLPSGDIARAEERRLAARDVADALD
LPIGNAVDFWTEASLFSAGGYTALVYGPGDIAQAHTADEFVTLAQLQRYV
ESVNRIINGS
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain2f7v Chain A Residue 5367 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2f7v Structure of a novel N-acetyl-L-citrulline deacetylase from Xanthomonas campestris
Resolution1.75 Å
Binding residue
(original residue number in PDB)		H72 D103 E130 E155
Binding residue
(residue number reindexed from 1)		H73 D104 E131 E156
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.-
Gene Ontology
Molecular Function
GO:0008777 acetylornithine deacetylase activity
GO:0016787 hydrolase activity
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0019213 deacetylase activity
GO:0043909 N-acetylcitrulline deacetylase activity
GO:0046872 metal ion binding
GO:0050897 cobalt ion binding
Biological Process
GO:0006526 L-arginine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2f7v, PDBe:2f7v, PDBj:2f7v
PDBsum2f7v
PubMed16750290
UniProtQ8P8J5|ACDAS_XANCP N-acetyl-L-citrulline deacetylase (Gene Name=argE')

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