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1J3G

Solution structure of Citrobacter Freundii AmpD

Replaces:  1IYAReplaces:  1J2S
Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
A0009253biological_processpeptidoglycan catabolic process
A0009254biological_processpeptidoglycan turnover
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 210
ChainResidue
AHIS34
AHIS154
AASP164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues137
DetailsDomain: {"description":"N-acetylmuramoyl-L-alanine amidase","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P75820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12654266","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P75820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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