1f4v

X-ray diffraction
2.22Å resolution

CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chemotaxis protein CheY Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 128 amino acids
Theoretical weight: 13.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AE67 (Residues: 2-129; Coverage: 99%)
Gene names: JW1871, b1882, cheY
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold
Flagellar motor switch protein FliM Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 16 amino acids
Theoretical weight: 1.69 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P06974 (Residues: 1-16; Coverage: 5%)
Gene names: JW1929, b1945, cheC2, fla AII, fla QII, fliM

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P3221
Unit cell:
a: 54.232Å b: 54.233Å c: 347.433Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.217 0.258
Expression system: Escherichia coli