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3D2Y

Complex of the N-acetylmuramyl-L-alanine amidase AmiD from E.coli with the substrate anhydro-N-acetylmuramic acid-L-Ala-D-gamma-Glu-L-Lys

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
A0009253biological_processpeptidoglycan catabolic process
A0009254biological_processpeptidoglycan turnover
A0009279cellular_componentcell outer membrane
A0009392molecular_functionN-acetyl-anhydromuramoyl-L-alanine amidase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019867cellular_componentouter membrane
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 262
ChainResidue
ATHR18
AARG20
AGLN21
AGLN74
ALEU75
AVAL76
APRO77
AHOH499

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 263
ChainResidue
AALA172
AGLN173
ATRP179
AASP181
ALYS257
AGLN169

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":"PubMed","id":"20036252","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20036252","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"20036252","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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