› 5acu

X-ray diffraction
2.1Å resolution

VIM-2-NAT, Discovery of novel inhibitor scaffolds against the metallo- beta-lactamase VIM-2 by SPR based fragment screening

Released:
DOI: 10.2210/pdb5acu/pdb
PDB entry 5acu coloured by chain, front view.
PDB entry 5acu coloured by chain, side view.
PDB entry 5acu coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Discovery of Novel Inhibitor Scaffolds against the Metallo-β-lactamase VIM-2 by Surface Plasmon Resonance (SPR) Based Fragment Screening.
Christopeit T, Carlsen TJ, Helland R, Leiros HK
J Med Chem 58 8671-82 (2015)
PMID: 26477515

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
  • not assigned
Biological process:
  • not assigned
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 Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 28.35 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K2N0 (Residues: 1-266; Coverage: 100%)
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 OH 1 x OH
Ligand ZN 3 x ZN
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 64.422Å b: 75.795Å c: 79.292Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.256 0.287
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
5 more

2 mentions without citation

The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.
Christopeit et al. (2016)
1 more