PDBe 1u0s

X-ray diffraction
1.9Å resolution

Chemotaxis kinase CheA P2 domain in complex with response regulator CheY from the thermophile thermotoga maritima

Released:
Source organism: Thermotoga maritima

Function and Biology Details

Reaction catalysed:
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chemotaxis protein CheA Chain: A
Molecule details ›
Chain: A
Length: 86 amino acids
Theoretical weight: 9.98 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56310 (Residues: 175-260; Coverage: 13%)
Gene names: TM_0702, cheA
Sequence domains: P2 response regulator binding domain
Structure domains: CheY-binding domain of CheA. Chain A
Chemotaxis protein CheY Chain: Y
Molecule details ›
Chain: Y
Length: 118 amino acids
Theoretical weight: 12.97 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56312 (Residues: 2-119; Coverage: 98%)
Gene names: TM_0700, 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
X-ray source: CHESS BEAMLINE F2
Spacegroup: P21212
Unit cell:
a: 88.55Å b: 91.43Å c: 31.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.253
Expression system: Escherichia coli BL21(DE3)