› 7ljk

X-ray diffraction
1.81Å resolution

Crystal structure of the deacylation deficient KPC-2 F72Y mutant

Released:
DOI: 10.2210/pdb7ljk/pdb
PDB entry 7ljk coloured by chain, front view.
PDB entry 7ljk coloured by chain, side view.
PDB entry 7ljk coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
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 IM, Mehta SC, Sankaran B, Hu L, Prasad BVV, Palzkill T
OpenAccess logo J Biol Chem 296 100799
PMID: 34022225

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-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 28.01 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F663 (Residues: 26-289; Coverage: 98%)
Gene names: KPC-1, KPC-2, bla, kpc, kpc1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P1
Unit cell:
a: 34.325Å b: 37.31Å c: 82.178Å
α: 92.43° β: 90.413° γ: 94.617°
R-values:
R R work R free
0.159 0.157 0.197
Expression system: Escherichia coli

Quick links

Citations

3 review citations

β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.
Mora-Ochomogo et al. (2021)
2 more

1 mention without citation

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)