X-ray diffraction
1.85Å resolution

Crystal structure of the Class A beta-lactamase L2 from Stenotrophomonas maltophilia

Source organism: Stenotrophomonas maltophilia
Entry authors: Pernot L, Petrella S, Sougakoff W

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 276 amino acids
Theoretical weight: 29.16 KDa
Source organism: Stenotrophomonas maltophilia
Expression system: Escherichia coli BL21
  • Canonical: Q9RBQ1 (Residues: 28-303; Coverage: 100%)
Gene names: L2, blaL2
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P41212
Unit cell:
a: 135.503Å b: 135.503Å c: 94.856Å
α: 90° β: 90° γ: 90°
R R work R free
0.164 0.147 0.164
Expression system: Escherichia coli BL21