› 7llb

X-ray diffraction
1.67Å resolution

Crystal structure of KPC-2 S70G/T215P mutant with hydrolyzed meropenem

Released:
DOI: 10.2210/pdb7llb/pdb
PDB entry 7llb coloured by chain, front view.
PDB entry 7llb coloured by chain, side view.
PDB entry 7llb 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
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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 27.96 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F663 (Residues: 26-289; Coverage: 98%)
Gene names: bla, kpc, kpc1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand 8YL 2 x 8YL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P1
Unit cell:
a: 34.495Å b: 37.292Å c: 82.128Å
α: 91.391° β: 90.372° γ: 93.789°
R-values:
R R work R free
0.172 0.171 0.193
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)