1i5d

X-ray diffraction
2.9Å resolution

STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH TNP-ATP

Released:
Source organism: Thermotoga maritima
Primary publication:
Nucleotide binding by the histidine kinase CheA.
Nat Struct Biol 8 353-60 (2001)
PMID: 11276258

Function and Biology Details

Reaction catalysed:
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-176348 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chemotaxis protein CheA Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 21.43 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56310 (Residues: 350-540; Coverage: 29%)
Gene names: TM_0702, cheA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P4322
Unit cell:
a: 85.19Å b: 85.19Å c: 73.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.263 0.263 0.312
Expression system: Escherichia coli BL21(DE3)