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6LBL

Crystal structure of IMP-1 metallo-beta-lactamase in complex with NO9 inhibitor

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 301
ChainResidue
AHIS77
AHIS79
AHIS139
AZN302
ANO9304

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
ANO9304
AASP81
ACYS158
AHIS197
AZN301

site_idAC3
Number of Residues7
Detailsbinding site for residue NA A 303
ChainResidue
AASN90
AILE94
APRO95
ATHR96
ATHR115
AHOH517
AHOH603

site_idAC4
Number of Residues14
Detailsbinding site for residue NO9 A 304
ChainResidue
AVAL25
AHIS77
AHIS79
AASP81
AHIS139
ACYS158
ALYS161
AGLY166
AASN167
AHIS197
AZN301
AZN302
AHOH420
AHOH433

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsr.S
ChainResidueDetails
AILE74-SER93

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PerkILfGgCFIK
ChainResidueDetails
APRO149-LYS161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303
ChainResidueDetails
AHIS77
AHIS79
AASP81
AHIS139
ACYS158
ALYS161
AHIS197

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASN167

237735

PDB entries from 2025-06-18

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