› 4fr7

X-ray diffraction
1.61Å resolution

Crystal structure of the metallo-beta-lactamase VIM-31 in its reduced form at 1.61 A

Released:
DOI: 10.2210/pdb4fr7/pdb
PDB entry 4fr7 coloured by chain, front view.
PDB entry 4fr7 coloured by chain, side view.
PDB entry 4fr7 coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
The three-dimensional structure of VIM-31--a metallo-β-lactamase from Enterobacter cloacae in its native and oxidized form.
Kupper MB, Herzog K, Bennink S, Schlömer P, Bogaerts P, Glupczynski Y, Fischer R, Bebrone C, Hoffmann KM
FEBS J 282 2352-60 (2015)
PMID: 25825035

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-125088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 25.19 KDa
Source organism: Enterobacter cloacae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: I3RJZ3 (Residues: 31-266; Coverage: 96%)
Gene name: blaVIM-31
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 2 x ACT
Ligand CL 1 x CL
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: I222
Unit cell:
a: 64.6Å b: 74.39Å c: 78.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.186
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Metallo-ß-lactamases: a review.
Behzadi et al. (2020)
2 more

2 mentions without citation

Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.
Aitha et al. (2014)
1 more