› 2hp5

X-ray diffraction
2.7Å resolution

Crystal Structure of the OXA-10 W154G mutant at pH 7.0

Released:
DOI: 10.2210/pdb2hp5/pdb
PDB entry 2hp5 coloured by chain, front view.
PDB entry 2hp5 coloured by chain, side view.
PDB entry 2hp5 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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 248 amino acids
Theoretical weight: 27.58 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

2 bound ligands:
Ligand SO4 10 x SO4
Ligand CO 4 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 47.11Å b: 125.4Å c: 92.36Å
α: 90° β: 99.8° γ: 90°
R-values:
R R work R free
0.213 0.21 0.267
Expression system: Escherichia coli

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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

Active site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.
Chakraborty et al. (2011)