› 2rl3

X-ray diffraction
1.9Å resolution

Crystal structure of the OXA-10 W154H mutant at pH 7

Released:
DOI: 10.2210/pdb2rl3/pdb
PDB entry 2rl3 coloured by chain, front view.
PDB entry 2rl3 coloured by chain, side view.
PDB entry 2rl3 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:
  • not assigned
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: 27.66 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P14489 (Residues: 20-266; Coverage: 100%)
Gene names: bla, oxa10, pse2
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
Ligand SO4 5 x SO4
Ligand GOL 7 x GOL
Ligand EDO 1 x EDO
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 48.68Å b: 97.06Å c: 125.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.218
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

1 mention without citation

Ice nucleation in a Gram-positive bacterium isolated from precipitation depends on a polyketide synthase and non-ribosomal peptide synthetase.
Failor et al. (2022)