› 5mxr

X-ray diffraction
1.75Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 24.77 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K2N0 (Residues: 32-263; Coverage: 94%)
Gene names: PAERUG_P19_London_7_VIM_2_05_10_01672, bla vim-2, blaVIM-2, blm
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

3 bound ligands:
Ligand ZN 3 x ZN
Ligand ACT 1 x ACT
Ligand JTY 2 x JTY
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: I222
Unit cell:
a: 67.65Å b: 78.38Å c: 78.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Metallo-β-Lactamases: Structure, Function, Epidemiology, Treatment Options, and the Development Pipeline.
Boyd et al. (2020)
2 more

1 mention without citation

SAR Studies Leading to the Identification of a Novel Series of Metallo-β-lactamase Inhibitors for the Treatment of Carbapenem-Resistant Enterobacteriaceae Infections That Display Efficacy in an Animal Infection Model.
Leiris et al. (2019)