1f9n

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF AHRC, THE ARGININE REPRESSOR/ACTIVATOR PROTEIN FROM BACILLUS SUBTILIS

Released:
Source organism: Bacillus subtilis
Primary publication:
The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis.
Acta Crystallogr. D Biol. Crystallogr. 58 421-30 (2002)
PMID: 11856827

Function and Biology Details

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine repressor Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 149 amino acids
Theoretical weight: 16.85 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P17893 (Residues: 1-149; Coverage: 100%)
Gene names: BSU24250, ahrC, argR
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2221
Unit cell:
a: 230.31Å b: 73.86Å c: 138.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.27
Expression system: Escherichia coli