› 2y8a

X-ray diffraction
2.33Å resolution

VIM-7 with Oxidised. Structural and computational investigations of VIM-7: Insights into the substrate specificity of VIM metallo-beta- lactamases

Released:
DOI: 10.2210/pdb2y8a/pdb
PDB entry 2y8a coloured by chain, front view.
PDB entry 2y8a coloured by chain, side view.
PDB entry 2y8a coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structural and computational investigations of VIM-7: insights into the substrate specificity of vim metallo-β-lactamases.
Borra PS, Leiros HK, Ahmad R, Spencer J, Leiros I, Walsh TR, Sundsfjord A, Samuelsen O
J Mol Biol 411 174-89 (2011)
PMID: 21645522

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182987 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 28.14 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q840P9 (Residues: 1-265; Coverage: 100%)
Gene name: blaVIM-7
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 1 x MG
Ligand UNX 1 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P43
Unit cell:
a: 70.138Å b: 70.138Å c: 47.529Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.187 0.254
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

1 mention without citation

His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency of the metallo-β-lactamase VIM-7.
Leiros et al. (2014)