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4F6H

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
ASO4304

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 302
ChainResidue
ASER198
AHOH535
AILE160
ALYS161
APRO162
ASER196
AHIS197

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 303
ChainResidue
ATRP124
AGLU131
ALYS186
AHOH514
AHOH542

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AHIS77
AHIS79
AASP81
AHIS139
ALYS161
ASER196
AHIS197
AZN301

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ALYS11
ATYR17
ATRP28
AGLN233
APHE234
AGLU235
AHOH504
AHOH545
AHOH547

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

237735

PDB entries from 2025-06-18

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