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4HKY

New Delhi Metallo-beta-Lactamase-1, Complexed with Cd and Faropenem

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 Residues11
DetailsBINDING SITE FOR RESIDUE FPM A 301
ChainResidue
ATRP93
ACD304
AHOH417
AHIS122
AASP124
AHIS189
ACYS208
ALYS211
AASN220
AHIS250
ACD303

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SFR A 302
ChainResidue
ATRP93
AHIS122
AASP124
ALYS211
AGLY219
AASN220
AHIS250
ACD303
ACD304

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CD A 303
ChainResidue
AHIS120
AHIS122
AHIS189
ACYS208
AFPM301
ASFR302
ACD304

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 304
ChainResidue
AASP124
ACYS208
AHIS250
AFPM301
ASFR302
ACD303

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 305
ChainResidue
AGLU152
AASP223
AHOH431
BGLU227

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 306
ChainResidue
APHE240
APRO241
ALYS242
AALA243

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 307
ChainResidue
ALYS216

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SFR B 301
ChainResidue
BGLY69
BPHE70
BHIS122
BASP124
BHIS189
BLYS211
BGLY219
BASN220
BHIS250
BCD305
BCD306

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FPM B 302
ChainResidue
BGLY69
BPHE70
BTRP93
BHIS122
BASP124
BHIS189
BLYS211
BGLY219
BASN220
BHIS250
BCD305
BCD306

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
BARG32

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 304
ChainResidue
AASP48
BARG32
BARG45
BHOH487

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CD B 305
ChainResidue
BHIS120
BHIS122
BASP124
BHIS189
BCYS208
BSFR301
BFPM302
BCD306

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD B 306
ChainResidue
BASP124
BCYS208
BHIS250
BSFR301
BFPM302
BCD305

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD B 307
ChainResidue
AGLU227
BGLU152
BASP223
BHOH465

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 308
ChainResidue
BPHE240
BPRO241
BLYS242
BALA243
BHOH475

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 309
ChainResidue
BLYS216

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

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PDB entries from 2024-07-24

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