3zxq

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF THE ATP-BINDING DOMAIN OF MYCOBACTERIUM TUBERCULOSIS DOST

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-161493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxygen sensor histidine kinase response regulator DosT Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 13.26 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WGK1 (Residues: 451-573; Coverage: 22%)
Gene names: Rv2027c, dosT
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P212121
Unit cell:
a: 50.914Å b: 65.867Å c: 72.704Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.232
Expression system: Escherichia coli BL21(DE3)