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4F6Z

Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-b-lactamase active site

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS77
AHIS79
AHIS139
AFLC302

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE FLC A 302
ChainResidue
AGLY158
ALYS161
AASN167
ASER196
AHIS197
AZN301
AHOH449
ALYS33
AHIS77
AHIS79
AASP81
AHIS139

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

219140

PDB entries from 2024-05-01

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