4e04

X-ray diffraction
1.79Å resolution

RpBphP2 chromophore-binding domain crystallized by homologue-directed mutagenesis.

Released:
Entry authors: Bellini D, Papiz MZ

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 327 amino acids
Theoretical weight: 36.19 KDa
Source organism: Rhodopseudomonas palustris CGA009
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6N5G3 (Residues: 1-104, 105-318; Coverage: 42%)
Gene names: RPA3015, phyB1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 52.35Å b: 79.86Å c: 149.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.232
Expression system: Escherichia coli