X-ray diffraction
1.85Å resolution

Crystal structure of the KPC-2 carbapenemase


Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Carbapenem-hydrolyzing beta-lactamase KPC Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 261 amino acids
Theoretical weight: 27.66 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli str. K-12 substr. DH10B
  • Canonical: Q9F663 (Residues: 30-290; Coverage: 97%)
Gene names: bla, kpc, kpc1
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P31
Unit cell:
a: 116.245Å b: 116.245Å c: 52.001Å
α: 90° β: 90° γ: 120°
R R work R free
0.148 0.148 0.19
Expression system: Escherichia coli str. K-12 substr. DH10B