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4HL2

New Delhi Metallo-beta-Lactamase-1 1.05 A structure Complexed with Hydrolyzed Ampicillin

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 Residues20
DetailsBINDING SITE FOR RESIDUE ZZ7 A 301
ChainResidue
ALEU65
AGLY219
AASN220
AHIS250
AZN302
AZN303
AHOH416
AHOH458
AHOH701
BTHR34
BPRO68
AMET67
BGLY69
ATRP93
AHIS122
AGLN123
AASP124
AHIS189
ACYS208
ALYS211

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHIS120
AHIS122
AHIS189
AZZ7301
AHOH701

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
AASP124
ACYS208
AHIS250
AZZ7301
AHOH701

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
APRO112
AVAL113
AEDO305
AHOH460

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AASN57
ALYS106
APRO112
AGLY200
AEDO304
AHOH424
AHOH499
AHOH560
AHOH682

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AASP82
AALA134
AALA135
AHOH628

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
AARG234
AHOH472
AHOH488
BEDO306
BHOH518

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
AASP223
AALA224
AHOH426
BALA224
BASP225
BHOH436
BHOH614

site_idAC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ZZ7 B 302
ChainResidue
ATHR34
APRO68
AGLY69
BLEU65
BMET67
BTRP93
BHIS122
BGLN123
BASP124
BHIS189
BCYS208
BLYS211
BGLY219
BASN220
BHIS250
BZN303
BZN304
BHOH410
BHOH431
BHOH461
BHOH589
BHOH600
BHOH687

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 303
ChainResidue
BHIS120
BHIS122
BHIS189
BZZ7302
BHOH687

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 304
ChainResidue
BASP124
BCYS208
BHIS250
BZZ7302
BHOH687

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 305
ChainResidue
AGLU227
BGLU152
BASP223
BHOH688

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO B 306
ChainResidue
AHOH521
BARG234
BALA235
BALA238
BHOH427
BHOH428
AARG234
AASP267
AEDO307

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 307
ChainResidue
AGLY71
AHOH503
AHOH698
BASN220
BLEU221
BGLY222
BHOH670

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 2024-08-07

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