3k1j

X-ray diffraction
2Å resolution

Crystal structure of Lon protease from Thermococcus onnurineus NA1

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Archaeal Lon protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 604 amino acids
Theoretical weight: 66.78 KDa
Source organism: Thermococcus onnurineus NA1
Expression system: Escherichia coli
UniProt:
  • Canonical: B6YU74 (Residues: 1-635; Coverage: 94%)
Gene name: TON_0529
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P63
Unit cell:
a: 121.454Å b: 121.454Å c: 195.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.235
Expression system: Escherichia coli