8oz9

X-ray diffraction
1.4Å resolution

Structure of the Histidine Kinase CheA ATP-Binding domain in complex with compound QUI-SV-383

Released:
Source organism: Thermotoga maritima
Entry authors: Adhav A, Marina A

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 189 amino acids
Theoretical weight: 21.08 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56310 (Residues: 355-540; Coverage: 28%)
Gene names: TM_0702, cheA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21
Unit cell:
a: 41.113Å b: 59.773Å c: 66.609Å
α: 90° β: 97.154° γ: 90°
R-values:
R R work R free
0.159 0.158 0.193
Expression system: Escherichia coli BL21(DE3)