X-ray diffraction
2.4Å resolution

Crystal structure of Aspartyl phosphate phosphatase F from Bacillus subtilis


Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Response regulator aspartate phosphatase F Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 45.79 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
  • Canonical: P71002 (Residues: 1-381; Coverage: 100%)
Gene names: BSU37460, rapF, ywhJ
Sequence domains:
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 97.21Å b: 97.21Å c: 203.155Å
α: 90° β: 90° γ: 120°
R R work R free
0.204 0.202 0.24
Expression system: Escherichia coli