› 7tbx

X-ray diffraction
3.16Å 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: 267 amino acids
Theoretical weight: 28.33 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F663 (Residues: 23-289; Coverage: 99%)
Gene names: bla, kpc, kpc1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-2
Spacegroup: C2
Unit cell:
a: 123.262Å b: 88.248Å c: 77.046Å
α: 90° β: 109.76° γ: 90°
R-values:
R R work R free
0.249 0.247 0.292
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Klebsiella pneumoniae Carbapenemase Variants Resistant to Ceftazidime-Avibactam: an Evolutionary Overview.
Hobson et al. (2022)
3 more

1 mention without citation

Structural Characterization of the D179N and D179Y Variants of KPC-2 β-Lactamase: Ω-Loop Destabilization as a Mechanism of Resistance to Ceftazidime-Avibactam.
Alsenani et al. (2022)