› 4uws

X-ray diffraction
1.66Å resolution

VIM-26-PEG. Leu224 in VIM-26 from Klebsiella pneumoniae has implications for drug binding.

Released:
DOI: 10.2210/pdb4uws/pdb
PDB 4uws coloured by chain and viewed from the front.
PDB 4uws coloured by chain and viewed from the side.
PDB 4uws coloured by chain and viewed from the top.
Source organism: Klebsiella pneumoniae
Primary publication:
Structural and biochemical characterization of VIM-26 show that Leu224 has implications for the substrate specificity of VIM metallo-��-lactamases.
Leiros HK, Edvardsen KS, Bjerga GE, Samuelsen Ø
FEBS J. (2015)
PMID: 25601024

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactamase_B domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 266 amino acids
Theoretical weight: 28.07 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E5BDC6 (Residues: 1-266; Coverage: 100%)
Gene name: blaVIM-26
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

4 bound ligands:
Ligand SO4 1 x SO4
Ligand ZN 2 x ZN
Ligand PEG 1 x PEG
Ligand EDO 1 x EDO
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 39.759Å b: 68.172Å c: 40.406Å
α: 90° β: 92.56° γ: 90°
R-values:
R R work R free
0.158 0.156 0.2
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
1 more