› 1udr

X-ray diffraction
1.9Å resolution

CHEY MUTANT WITH LYS 91 REPLACED BY ASP, LYS 92 REPLACED BY ALA, ILE 96 REPLACED BY LYS AND ALA 98 REPLACED BY LEU (STABILIZING MUTATIONS IN HELIX 4)

Released:
DOI: 10.2210/pdb1udr/pdb
PDB entry 1udr coloured by chain, front view.
PDB entry 1udr coloured by chain, side view.
PDB entry 1udr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY.
Solà M, López-Hernández E, Cronet P, Lacroix E, Serrano L, Coll M, Párraga A
J Mol Biol 303 213-25 (2000)
PMID: 11023787

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142408 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chemotaxis protein CheY Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 129 amino acids
Theoretical weight: 14.18 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE67 (Residues: 1-129; Coverage: 100%)
Gene names: JW1871, b1882, cheY
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 53.85Å b: 109.76Å c: 54Å
α: 90° β: 111.09° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Insights from coarse-grained Gō models for protein folding and dynamics.
Hills et al. (2009)
21 other articles