› 4q0h

X-ray diffraction
1.16Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacteriophytochrome Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 37.02 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RZA4 (Residues: 1-321; Coverage: 43%)
Gene names: DR_A0050, bphP
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand IPA 3 x IPA
Ligand LBV 1 x LBV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 89.536Å b: 51.608Å c: 80.633Å
α: 90° β: 116.32° γ: 90°
R-values:
R R work R free
0.131 0.131 0.157
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Phytochromes: an atomic perspective on photoactivation and signaling.
Burgie et al. (2014)
6 more

4 mentions without citation

Crystallographic and electron microscopic analyses of a bacterial phytochrome reveal local and global rearrangements during photoconversion.
Burgie et al. (2014)
3 more