› 2fmk

X-ray diffraction
2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-531571 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chemotaxis protein CheY Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.14 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2D5 (Residues: 1-129; Coverage: 100%)
Gene names: STM1916, cheY
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold
Protein phosphatase CheZ Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.65 KDa
Source organism: Salmonella enterica subsp. enterica serovar Choleraesuis str. SC-B67
Expression system: Not provided
UniProt:
  • Canonical: Q57N83 (Residues: 174-188; Coverage: 8%)
Gene names: SCH_1922, cheZ

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand BEF 1 x BEF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 54.189Å b: 61.953Å c: 36.617Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.186 0.232
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Bacterial response regulators: versatile regulatory strategies from common domains.
Gao et al. (2007)
1 more

4 mentions without citation

Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.
Guhaniyogi et al. (2006)
3 more