5ni0

X-ray diffraction
1.67Å resolution

VIM-2_10c. Metallo-beta-Lactamase Inhibitors by Bioisosteric Replacement: Preparation, Activity and Binding

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactamase_B domain-containing protein Chains: A, E
Molecule details ›
Chains: A, E
Length: 266 amino acids
Theoretical weight: 28.35 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9K2N0 (Residues: 1-266; Coverage: 100%)
Gene names: VIM-2, bla vim-2, bla-VIM-2, blaVIM-2, blaVIM2, blasVIM-2, vim-2
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 45.716Å b: 91.07Å c: 122.912Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.214
Expression system: Escherichia coli