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3ZR9

Structure of New Delhi Metallo-Beta-lactamase 1 (NDM-1)

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 273
ChainResidue
AHIS120
AHIS122
AHIS189
ACD276
AHOH2043

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 274
ChainResidue
AHOH2031
AHOH2051
AASP95
AASP130
AHOH2029
AHOH2030

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 275
ChainResidue
AHIS228
AHOH2102

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CD A 276
ChainResidue
AASP124
ACYS208
AHIS250
AZN273
AHOH2043
AHOH2048
AHOH2090

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 277
ChainResidue
AHIS159
AHIS159

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 278
ChainResidue
AHIS261
AHOH2113
AHOH2115
AHOH2116

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI A 279
ChainResidue
AGLU152
AGLU170
AASP223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530
ChainResidueDetails
AHIS120
AHIS122
AASP124
AHIS189
ACYS208
AHIS250

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22713171
ChainResidueDetails
ALYS211
AASN220

226262

PDB entries from 2024-10-16

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