› 1m6k

X-ray diffraction
1.5Å resolution

Structure of the OXA-1 class D beta-lactamase

Released:
DOI: 10.2210/pdb1m6k/pdb
PDB entry 1m6k coloured by chain, front view.
PDB entry 1m6k coloured by chain, side view.
PDB entry 1m6k coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Comparison of beta-lactamases of classes A and D: 1.5-A crystallographic structure of the class D OXA-1 oxacillinase.
Sun T, Nukaga M, Mayama K, Braswell EH, Knox JR
Protein Sci 12 82-91 (2003)
PMID: 12493831

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146686 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase OXA-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 251 amino acids
Theoretical weight: 28.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P13661 (Residues: 26-276; Coverage: 100%)
Gene names: bla, oxa1
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand MPD 10 x MPD
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P1
Unit cell:
a: 36.02Å b: 51.62Å c: 72.89Å
α: 70.19° β: 84.11° γ: 81.51°
R-values:
R R work R free
0.182 0.182 0.203
Expression system: Escherichia coli BL21

Quick links

Citations

11 review citations

OXA-type carbapenemases.
Walther-Rasmussen et al. (2006)
10 more

17 mentions without citation

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
16 more