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4UBQ

Crystal Structure of IMP-2 Metallo-beta-Lactamase from Acinetobacter spp.

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS78
AHIS80
AHIS140
AZN302
AACT303

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AACT303
AASP82
ACYS159
AHIS198
AZN301

site_idAC3
Number of Residues10
Detailsbinding site for residue ACT A 303
ChainResidue
AHIS80
ALYS128
AHIS140
ALYS162
AASN168
AHIS198
AZN301
AZN302
AHOH407
AHOH511

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsq.S
ChainResidueDetails
AILE75-SER94

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PekkILfGgCFVK
ChainResidueDetails
APRO150-LYS162

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PDB entries from 2026-03-11

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