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4RBS

Crystal Structure of New Delhi Metallo-beta-Lactamase-1 in the Complex with Hydrolyzed Meropenem

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 ZN A 300
ChainResidue
AHIS120
AHIS122
AHIS189
A0RV302

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AASP124
ACYS208
AHIS250
A0RV302

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 0RV A 302
ChainResidue
AHIS122
AASP124
AHIS189
ACYS208
ALYS211
AGLY219
AASN220
AHIS250
AZN300
AZN301
BGLY69
B0RV302
ATRP93

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 303
ChainResidue
APRO112
AVAL113
AHOH448

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AASN166
ATRP168
APHE183
AALA235
AALA238
AALA239

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
AARG256
AILE259
ATHR260

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BHIS120
BHIS122
BHIS189
B0RV302

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BASP124
BCYS208
BHIS250
B0RV302

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0RV B 302
ChainResidue
AGLY69
APHE70
A0RV302
BHIS122
BGLN123
BASP124
BHIS189
BCYS208
BLYS211
BGLY219
BASN220
BHIS250
BZN300
BZN301

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY B 303
ChainResidue
BARG85
BALA114
BASN176
BHOH432

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY B 304
ChainResidue
BPRO112
BVAL113
BALA135

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 305
ChainResidue
BASN166
BTRP168
BPHE183
BALA235
BALA238
BALA239

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 306
ChainResidue
BASN57
BARG81
BILE198
BTHR201
BHOH422

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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