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2F7V

Structure of acetylcitrulline deacetylase complexed with one Co

Functional Information from GO Data
ChainGOidnamespacecontents
A0006526biological_processL-arginine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0008777molecular_functionacetylornithine deacetylase activity
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0019213molecular_functiondeacetylase activity
A0043909molecular_functionN-acetylcitrulline deacetylase activity
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 5367
ChainResidue
AHIS72
AASP103
AGLU130
AGLU155
AHOH5461

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"16750290","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16750290","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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