› 5fqc

X-ray diffraction
1.45Å resolution

Crystal structure of the metallo-beta-lactamase VIM-2 with 2C

Released:
DOI: 10.2210/pdb5fqc/pdb
PDB entry 5fqc coloured by chain, front view.
PDB entry 5fqc coloured by chain, side view.
PDB entry 5fqc coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates.
Brem J, Cain R, Cahill S, McDonough MA, Clifton IJ, Jiménez-Castellanos JC, Avison MB, Spencer J, Fishwick CW, Schofield CJ
Nat Commun 7 12406 (2016)
PMID: 27499424

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-191748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 242 amino acids
Theoretical weight: 25.69 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K2N0 (Residues: 27-266; Coverage: 98%)
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

4 bound ligands:
Ligand FMT 4 x FMT
Ligand ZN 6 x ZN
Ligand OK3 2 x OK3
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 101.931Å b: 79.152Å c: 67.135Å
α: 90° β: 130.16° γ: 90°
R-values:
R R work R free
0.156 0.155 0.184
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

21 review citations

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

9 mentions without citation

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
8 more