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5EWA

Crystal structure of the metallo-beta-lactamase IMP-1 in complex with the bisthiazolidine inhibitor L-VC26

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 PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS77
AHIS79
AHIS139
AZN302
A9BZ303

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
A9BZ303
AASP81
ACYS158
AHIS197
AZN301

site_idAC3
Number of Residues13
Detailsbinding site for residue 9BZ A 303
ChainResidue
ATRP28
AHIS79
AASP81
AHIS139
ALYS161
AGLY166
AASN167
AHIS197
AZN301
AZN302
AEDO304
AHOH402
DGLU199

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO A 304
ChainResidue
A9BZ303
AHOH456

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS77
BHIS79
BHIS139
BZN302
B9BZ303

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN B 302
ChainResidue
BASP81
BCYS158
BHIS197
BZN301
B9BZ303

site_idAC7
Number of Residues11
Detailsbinding site for residue 9BZ B 303
ChainResidue
BVAL25
BTRP28
BHIS79
BASP81
BHIS139
BLYS161
BGLY166
BASN167
BHIS197
BZN301
BZN302

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS77
CHIS79
CHIS139
C9BZ304

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN C 302
ChainResidue
CASP81
CCYS158
CHIS197
C9BZ304

site_idAD1
Number of Residues5
Detailsbinding site for residue DMS C 303
ChainResidue
CSER119
CGLY120
CTYR134
CVAL144
CHOH420

site_idAD2
Number of Residues11
Detailsbinding site for residue 9BZ C 304
ChainResidue
CTRP28
CHIS79
CASP81
CHIS139
CLYS161
CASN167
CHIS197
CZN301
CZN302
CHOH404
CHOH407

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS77
DHIS79
DHIS139
DZN302

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN D 302
ChainResidue
DASP81
DCYS158
DHIS197
DZN301

site_idAD5
Number of Residues3
Detailsbinding site for residue 9BZ D 303
ChainResidue
DARG92
DLYS181
DVAL214

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 Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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