› 5hap

X-ray diffraction
1.89Å 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 27.95 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6XEC0 (Residues: 25-265; Coverage: 99%)
Gene names: KPE71T_00045, bla OXA-48, blaOXA-48
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

8 bound ligands:
Ligand CL 1 x CL
Ligand 1PE 1 x 1PE
Ligand PGE 2 x PGE
Ligand NA 2 x NA
Ligand PEG 8 x PEG
Ligand MPD 1 x MPD
Ligand PG4 1 x PG4
Ligand EDO 4 x EDO
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P6522
Unit cell:
a: 121.9Å b: 121.9Å c: 161.451Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.191 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Class C β-Lactamases: Molecular Characteristics.
Philippon et al. (2022)
10 other articles

3 mentions without citation

Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric Strain.
Stojanoski et al. (2016)
2 more