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6LHE

Crystal Structure of Gold-bound 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
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 Residues4
Detailsbinding site for residue AU A 301
ChainResidue
AGLU152
AASP223
AHOH557
BGLU227

site_idAC2
Number of Residues4
Detailsbinding site for residue AU A 302
ChainResidue
AASP124
ACYS208
AHIS250
AHOH568

site_idAC3
Number of Residues4
Detailsbinding site for residue AU A 303
ChainResidue
AHIS122
AHIS189
AHOH436
AHIS120

site_idAC4
Number of Residues11
Detailsbinding site for residue SO4 A 304
ChainResidue
AGLN158
AHIS159
ASER160
AHOH401
AHOH423
AHOH437
AHOH513
AHOH524
BHIS261
BARG264
BLYS268

site_idAC5
Number of Residues7
Detailsbinding site for residue SO4 A 305
ChainResidue
AARG234
ATHR260
AARG264
AHOH411
AHOH413
AHOH486
BGLN44

site_idAC6
Number of Residues4
Detailsbinding site for residue AU B 301
ChainResidue
AGLU227
BGLU152
BASP223
BHOH548

site_idAC7
Number of Residues4
Detailsbinding site for residue AU B 302
ChainResidue
BASP124
BCYS208
BHIS250
BHOH560

site_idAC8
Number of Residues3
Detailsbinding site for residue AU B 303
ChainResidue
BHIS120
BHIS122
BHIS189

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

223166

PDB entries from 2024-07-31

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