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6JED

Crystal structure of IMP-1 metallo-beta-lactamase in a complex with MCR

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
AMCR303

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AMCR303
AASP81
ACYS158
AHIS197
AZN301

site_idAC3
Number of Residues8
Detailsbinding site for residue MCR A 303
ChainResidue
AHIS79
AASP81
AHIS139
ACYS158
ALYS161
AHIS197
AZN301
AZN302

site_idAC4
Number of Residues9
Detailsbinding site for residue EPE A 304
ChainResidue
ATRP28
AGLU104
ALYS161
APRO162
ATYR163
AGLY164
AHIS197
ASER198
AHOH500

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
AASP81
AHIS139
ACYS158
ALYS161
AHIS197
AHIS77
AHIS79

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

219869

PDB entries from 2024-05-15

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