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4GYQ

Crystal Structure of New Delhi Metallo-beta-Lactamase-1 D223A mutant from Klebsiella pneumoniae

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
C0008270molecular_functionzinc ion binding
C0008800molecular_functionbeta-lactamase activity
C0017001biological_processantibiotic catabolic process
C0042597cellular_componentperiplasmic space
D0008270molecular_functionzinc ion binding
D0008800molecular_functionbeta-lactamase activity
D0017001biological_processantibiotic catabolic process
D0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
AGLY47
AASP48
ALEU49
AASP96
AGLN97
AGLN100
BARG45

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AASP202
AILE203
AALA243
AILE198
ATHR201

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BASP66
BMET126
BHOH614

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 301
ChainResidue
CGLY178
CHOH481
CHOH501
CHOH584
CHOH591

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25815530","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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