8sbm

X-ray diffraction
1.47Å resolution

Crystal structure of the wild-type Catalytic ATP-binding domain of Mtb DosS

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-274248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxygen sensor histidine kinase response regulator DevS/DosS Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 13.23 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WGK3 (Residues: 454-578; Coverage: 22%)
Gene names: Rv3132c, devS, dosS
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 54.438Å b: 61.775Å c: 72.234Å
α: 90° β: 107.54° γ: 90°
R-values:
R R work R free
0.155 0.153 0.193
Expression system: Escherichia coli