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3D2Z

Complex of the N-acetylmuramyl-L-alanine amidase AmiD from E.coli with the product 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
A0016787molecular_functionhydrolase activity
A0019867cellular_componentouter membrane
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS35
AHIS151
AASP161

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 263
ChainResidue
AASP17
AARG20

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS35
AHIS151
AASP161
AHOH322

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 263
ChainResidue
AASP17
AARG20
AHOH337

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:20036252
ChainResidueDetails
AGLU104

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20036252
ChainResidueDetails
AHIS35
AHIS151
AASP161

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ATYR36

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:20036252
ChainResidueDetails
ALYS159

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PDB entries from 2024-07-17

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