› 3byd

X-ray diffraction
1.93Å resolution

Crystal structure of beta-lactamase OXY-1-1 from Klebsiella oxytoca

Released:
DOI: 10.2210/pdb3byd/pdb
PDB entry 3byd coloured by chain, front view.
PDB entry 3byd coloured by chain, side view.
PDB entry 3byd coloured by chain, top view.
Source organism: Klebsiella oxytoca
Primary publication:
Structural insights into the broadened substrate profile of the extended-spectrum β-lactamase OXY-1-1 from Klebsiella oxytoca.
Liang YH, Gao R, Su XD
Acta Crystallogr D Biol Crystallogr 68 1460-7 (2012)
PMID: 23090395

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-149621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase OXY-1 Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 28.61 KDa
Source organism: Klebsiella oxytoca
Expression system: Escherichia coli
UniProt:
  • Canonical: P22391 (Residues: 25-291; Coverage: 100%)
Gene name: bla
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 46.545Å b: 73.431Å c: 84.561Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.182 0.225
Expression system: Escherichia coli

Quick links

Citations

1 review citation

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.
Philippon et al. (2016)

1 mention without citation

Influence of C-H...O interactions on the structural stability of β-lactamases.
Lavanya et al. (2013)