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8Z5L

Crystal structure of metallo-beta-lactamse, IMP-1, complexed with a quinolinone-based inhibitor

This is a non-PDB format compatible entry.
Replaces:  8Y0S
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
C0008270molecular_functionzinc ion binding
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0042597cellular_componentperiplasmic space
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
D0008270molecular_functionzinc ion binding
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0042597cellular_componentperiplasmic space
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsr.S
ChainResidueDetails
AILE78-SER97

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PerkILfGgCFIK
ChainResidueDetails
APRO153-LYS165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303
ChainResidueDetails
AHIS81
BASP85
BHIS143
BCYS162
BLYS165
BHIS201
CHIS81
CHIS83
CASP85
CHIS143
CCYS162
AHIS83
CLYS165
CHIS201
DHIS81
DHIS83
DASP85
DHIS143
DCYS162
DLYS165
DHIS201
AASP85
AHIS143
ACYS162
ALYS165
AHIS201
BHIS81
BHIS83

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P25910
ChainResidueDetails
AASN171
BASN171
CASN171
DASN171

222926

PDB entries from 2024-07-24

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