› 2xr0

X-ray diffraction
2.2Å resolution

Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase

Released:
DOI: 10.2210/pdb2xr0/pdb
PDB entry 2xr0 coloured by chain, front view.
PDB entry 2xr0 coloured by chain, side view.
PDB entry 2xr0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The active site protonation states of perdeuterated Toho-1 β-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation.
Tomanicek SJ, Wang KK, Weiss KL, Blakeley MP, Cooper J, Chen Y, Coates L
FEBS Lett 585 364-8 (2011)
PMID: 21168411

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175211 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Toho-1 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 27.99 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q47066 (Residues: 32-291; Coverage: 99%)
Gene name: bla
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 73.5Å b: 73.5Å c: 99.33Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.135 0.133 0.173
Expression system: Escherichia coli BL21

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Citations

4 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
3 more