› 2hpb

X-ray diffraction
2.05Å resolution

Crystal structure of the OXA-10 W154A mutant at pH 9.0

Released:
DOI: 10.2210/pdb2hpb/pdb
Model geometry
Fit model/data
PDB entry 2hpb coloured by chain, front view.
PDB entry 2hpb coloured by chain, side view.
PDB entry 2hpb coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Critical role of tryptophan 154 for the activity and stability of class D beta-lactamases.
Baurin S, Vercheval L, Bouillenne F, Falzone C, Brans A, Jacquamet L, Ferrer JL, Sauvage E, Dehareng D, Frère JM, Charlier P, Galleni M, Kerff F
Biochemistry 48 11252-63 (2009)
PMID: 19860471

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146960 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase OXA-10 Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 27.6 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P14489 (Residues: 20-266; Coverage: 100%)
Gene names: OXA-10, bla, oxa10, pse2
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 48.45Å b: 95.46Å c: 125.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.27
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from gram-negative bacteria.
Bush et al. (2011)
4 more