5h45

X-ray diffraction
2.7Å resolution

Crystal structure of the C-terminal Lon protease-like domain of Thermus thermophilus RadA/Sms

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair protein RadA Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 19.63 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SKV2 (Residues: 262-423; Coverage: 38%)
Gene names: TTHA0541, radA
Sequence domains: Subunit ChlI of Mg-chelatase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P4332
Unit cell:
a: 156.289Å b: 156.289Å c: 156.289Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.25
Expression system: Escherichia coli