› 2wyx

Neutron Diffraction
2.1Å resolution

Neutron structure of a class A Beta-lactamase Toho-1 E166A R274N R276N triple mutant

Released:
DOI: 10.2210/pdb2wyx/pdb
PDB entry 2wyx coloured by chain, front view.
PDB entry 2wyx coloured by chain, side view.
PDB entry 2wyx coloured by chain, top view.
Source organism: Escherichia coli BL21
Primary publication:
Neutron diffraction studies of a class A beta-lactamase Toho-1 E166A/R274N/R276N triple mutant.
Tomanicek SJ, Blakeley MP, Cooper J, Chen Y, Afonine PV, Coates L
J Mol Biol 396 1070-80 (2010)
PMID: 20036259

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: 256 amino acids
Theoretical weight: 27.5 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q47066 (Residues: 33-288; Coverage: 98%)
Gene name: bla
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand DOD 91 x DOD
No modified residues

Experiments and Validation Details

Spacegroup: P3221
Unit cell:
a: 72.993Å b: 72.993Å c: 98.365Å α: 90° β: 90° γ: 120°
R-values:
R R work R free 0.226 0.223 0.258
Expression system: Escherichia coli BL21

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Citations

2 review citations

Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from gram-negative bacteria.
Bush et al. (2011)
1 more

5 mentions without citation

Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition.
Liebschner et al. (2018)
4 more