X-ray diffraction
1.83Å resolution

Crystal structure of the PAS domain of nitrogen regulation protein NR(II) from Vibrio parahaemolyticus

Entry authors: Osipiuk J, Sather A, Abdullah J, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

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
histidine kinase Chain: A
Molecule details ›
Chain: A
Length: 115 amino acids
Theoretical weight: 12.85 KDa
Source organism: Vibrio parahaemolyticus RIMD 2210633
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q87TF0 (Residues: 1-112; Coverage: 32%)
Gene name: VP0119
Sequence domains: PAS fold
Structure domains: PAS domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6322
Unit cell:
a: 81.115Å b: 81.115Å c: 67.467Å
α: 90° β: 90° γ: 120°
R R work R free
0.184 0.184 0.196
Expression system: Escherichia coli BL21(DE3)