› 6b1f

X-ray diffraction
1.44Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190259 (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:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
Ligand C8Y 2 x C8Y
Ligand CIT 1 x CIT
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P1
Unit cell:
a: 34.54Å b: 37.432Å c: 82.339Å
α: 92.33° β: 90.05° γ: 95.25°
R-values:
R R work R free
0.151 0.15 0.174
Expression system: Escherichia coli

Quick links

Citations

28 review citations

New Carbapenemase Inhibitors: Clearing the Way for the β-Lactams.
Vázquez-Ucha et al. (2020)
27 more

2 mentions without citation

Influence of substrates and inhibitors on the structure of Klebsiella pneumoniae carbapenemase-2.
Shurina et al. (2019)
1 more