X-ray diffraction
1.03Å resolution

Apo structure of class a beta-lactamase Toho-1 R274N/R276N double mutant

Source organism: Escherichia coli
Primary publication:
Improvement of crystal quality by surface mutations of beta-lactamase Toho-1.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 379-82 (2009)
PMID: 19342785

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-lactamase Toho-1 Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 28.18 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: Q47066 (Residues: 30-291; Coverage: 100%)
Gene name: bla
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: SPRING-8 BEAMLINE BL26B1
Spacegroup: P3221
Unit cell:
a: 72.511Å b: 72.511Å c: 97.477Å
α: 90° β: 90° γ: 120°
R R work R free
0.138 0.138 0.148
Expression system: Escherichia coli