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6EX7

Crystal structure of NDM-1 metallo-beta-lactamase in complex with Cd ions and a hydrolyzed beta-lactam ligand - new refinement

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CD A 301
ChainResidue
AHIS120
AHIS122
AASP124
AHIS189
ACYS208
ACD302

site_idAC2
Number of Residues4
Detailsbinding site for residue CD A 302
ChainResidue
ACD301
AASP124
ACYS208
AHIS250

site_idAC3
Number of Residues5
Detailsbinding site for residue CD A 303
ChainResidue
AGLU152
AASP223
AHOH411
AHOH455
BGLU227

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 304
ChainResidue
APHE240
APRO241
ALYS242
AALA243

site_idAC5
Number of Residues4
Detailsbinding site for residue PG4 A 306
ChainResidue
AALA215
ALYS216
ALYS216
ASER217

site_idAC6
Number of Residues4
Detailsbinding site for residue CD A 307
ChainResidue
AGLU227
AHOH451
BGLU152
BASP223

site_idAC7
Number of Residues6
Detailsbinding site for residue CD B 301
ChainResidue
BHIS120
BHIS122
BASP124
BHIS189
BCYS208
BCD302

site_idAC8
Number of Residues4
Detailsbinding site for residue CD B 302
ChainResidue
BASP124
BCYS208
BHIS250
BCD301

site_idAC9
Number of Residues4
Detailsbinding site for residue CL B 303
ChainResidue
BPHE240
BPRO241
BLYS242
BALA243

site_idAD1
Number of Residues1
Detailsbinding site for residue CL B 304
ChainResidue
BLYS216

site_idAD2
Number of Residues6
Detailsbinding site for residue TOE B 306
ChainResidue
AGLY47
AASP48
BARG45
BGLY47
BASP48
BEDO307

site_idAD3
Number of Residues2
Detailsbinding site for residue EDO B 307
ChainResidue
BASP48
BTOE306

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25815530","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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