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7RSF

Acetylornithine deacetylase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006526biological_processL-arginine biosynthetic process
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0008777molecular_functionacetylornithine deacetylase activity
A0016787molecular_functionhydrolase activity
A0019213molecular_functiondeacetylase activity
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
B0005737cellular_componentcytoplasm
B0006526biological_processL-arginine biosynthetic process
B0008270molecular_functionzinc ion binding
B0008652biological_processamino acid biosynthetic process
B0008777molecular_functionacetylornithine deacetylase activity
B0016787molecular_functionhydrolase activity
B0019213molecular_functiondeacetylase activity
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
Functional Information from PROSITE/UniProt
site_idPS00758
Number of Residues10
DetailsARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. LLLAGHtDTV
ChainResidueDetails
ALEU75-VAL84

site_idPS00759
Number of Residues38
DetailsARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. TADmKGffAfiLdalrdvdvtklkkp...LyILAtaDEEtS
ChainResidueDetails
ATHR110-SER147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01108","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01108","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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