› 6xj8

X-ray diffraction
2.05Å resolution

KPC-2 N170A mutant bound to hydrolyzed imipenem at 2.05 A

Released:
DOI: 10.2210/pdb6xj8/pdb
PDB entry 6xj8 coloured by chain, front view.
PDB entry 6xj8 coloured by chain, side view.
PDB entry 6xj8 coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
KPC-2 β-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate.
Mehta SC, Furey IM, Pemberton OA, Boragine DM, Chen Y, Palzkill T
J Biol Chem 296 100155
PMID: 33273017

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 Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 31.1 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9F663 (Residues: 1-293; Coverage: 100%)
Gene names: bla, kpc, kpc1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand 8YF 1 x 8YF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Unit cell:
a: 56.599Å b: 59.36Å c: 77.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Local interactions with the Glu166 base and the conformation of an active site loop play key roles in carbapenem hydrolysis by the KPC-2 β-lactamase.
Furey et al. (2021)
6 more

2 mentions without citation

KPC-2 β-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate.
Mehta et al. (2021)
1 more