Structure of PDB 2f7v Chain A

Receptor sequence
>2f7vA (length=360) Species: 339 (Xanthomonas campestris) [Search protein sequence]
HMTDLLASTLEHLETLVSFDTRNPPRAIAAEGGIFDYLRAQLPGFQVEVI
DHGDGAVSLYAVRGTPKYLFNVHLDTVPDSPHWSADPHVMRRTEDRVIGL
GVCDIKGAAAALVAAANAGDGDAAFLFSSDEEANDPRCIAAFLARGLPYD
AVLVAEPTMSEAVLAHRGISSVLMRFAGRAGDPAASALHQAMRWGGKALD
HVESLAHARFGGLTGLRFNIGRVDGGIKANMIAPAAELRFGFRPLPSMDV
DGLLATFAGFADPAAAHFEETFRGPSLPSGDIARAEERRLAARDVADALD
LPIGNAVDFWTEASLFSAGGYTALVYGPGDIAQAHTADEFVTLAQLQRYV
ESVNRIINGS
3D structure
PDB2f7v Structure of a novel N-acetyl-L-citrulline deacetylase from Xanthomonas campestris
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.-
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 CO A H72 D103 E130 E155 H73 D104 E131 E156
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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