5n4s

X-ray diffraction
1.2Å resolution

VIM-2 metallo-beta-lactamase in complex with ((S)-3-mercapto-2-methylpropanoyl)-D-tryptophan (Compound 3)

Released:

Function and Biology Details

Biochemical function:
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, B
Molecule details ›
Chains: A, B
Length: 232 amino acids
Theoretical weight: 24.69 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K2N0 (Residues: 33-262; Coverage: 94%)
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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 103.845Å b: 80.308Å c: 68.732Å
α: 90° β: 130.34° γ: 90°
R-values:
R R work R free
0.185 0.184 0.2
Expression system: Escherichia coli BL21(DE3)