› 1ko2

X-ray diffraction
2.2Å resolution

VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with an oxidized Cys (cysteinesulfonic)

Released:
DOI: 10.2210/pdb1ko2/pdb
PDB entry 1ko2 coloured by chain, front view.
PDB entry 1ko2 coloured by chain, side view.
PDB entry 1ko2 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form.
Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O
J Mol Biol 375 604-11 (2008)
PMID: 18061205

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chain: A
Molecule details ›
Chain: A
Length: 230 amino acids
Theoretical weight: 24.57 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K2N0 (Residues: 32-261; 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

2 bound ligands:
Ligand ZN 2 x ZN
Ligand ACT 2 x ACT
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I222
Unit cell:
a: 67.18Å b: 78.03Å c: 80.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Metallo-β-lactamase structure and function.
Palzkill T. (2013)
9 more

6 mentions without citation

Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.
Jeon et al. (2015)
5 more