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5ZH1

Crystal structure of NDM-1 at pH7.5 (Imidazole) with 2 molecules per asymmetric unit

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 Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS120
AHIS122
AHIS189
AZN302
AOH303

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AOH303
AASP124
ACYS208
AHIS250
AZN301

site_idAC3
Number of Residues8
Detailsbinding site for residue OH A 303
ChainResidue
AHIS120
AHIS122
AASP124
AHIS189
ACYS208
AHIS250
AZN301
AZN302

site_idAC4
Number of Residues5
Detailsbinding site for residue IMD A 304
ChainResidue
AALA121
AGLU152
AASP192
AASP223
AHOH427

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS120
BHIS122
BHIS189
BZN302
BOH303

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN B 302
ChainResidue
BASP124
BCYS208
BHIS250
BZN301
BOH303

site_idAC7
Number of Residues10
Detailsbinding site for residue OH B 303
ChainResidue
BHIS120
BHIS122
BASP124
BHIS189
BCYS208
BHIS250
BZN301
BZN302
BHOH540
BHOH601

site_idAC8
Number of Residues4
Detailsbinding site for residue IMD B 304
ChainResidue
BALA121
BGLU152
BASP223
BHOH459

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530
ChainResidueDetails
AHIS120
BHIS189
BCYS208
BHIS250
AHIS122
AASP124
AHIS189
ACYS208
AHIS250
BHIS120
BHIS122
BASP124

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171
ChainResidueDetails
ALYS211
AASN220
BLYS211
BASN220

218853

PDB entries from 2024-04-24

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