6b1w

X-ray diffraction
1.73Å resolution

Crystal structure KPC-2 beta-lactamase complexed with WCK 5107 by co-crystallization

Released:
Source organism: Klebsiella pneumoniae
Entry authors: van den Akker F, Nguyen NQ

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbapenem-hydrolyzing beta-lactamase KPC Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 28.35 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F663 (Residues: 22-289; Coverage: 99%)
Gene names: bla, kpc, kpc1
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P1
Unit cell:
a: 34.528Å b: 37.348Å c: 82.068Å
α: 87.66° β: 89.71° γ: 84.31°
R-values:
R R work R free
0.154 0.152 0.194
Expression system: Escherichia coli