1ffs

X-ray diffraction
2.4Å resolution

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM CRYSTALS SOAKED IN ACETYL PHOSPHATE

Released:

Function and Biology Details

Reaction catalysed:
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chemotaxis protein CheY Chains: A, C
Molecule details ›
Chains: A, 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
Chemotaxis protein CheA Chains: B, D
Molecule details ›
Chains: B, D
Length: 134 amino acids
Theoretical weight: 14.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P07363 (Residues: 124-257; Coverage: 21%)
Gene names: JW1877, b1888, cheA
Sequence domains: CheY binding
Structure domains: CheY-binding domain of CheA

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P212121
Unit cell:
a: 159.3Å b: 53.4Å c: 77.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.217 0.255
Expression system: Escherichia coli