1us8

X-ray diffraction
2.1Å resolution

The Rad50 signature motif: essential to ATP binding and biological function

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157665 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA double-strand break repair Rad50 ATPase Chain: A
Molecule details ›
Chain: A
Length: 147 amino acids
Theoretical weight: 16.89 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P58301 (Residues: 1-147; Coverage: 17%)
Gene names: PF1167, rad50
Sequence domains: AAA domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
DNA double-strand break repair Rad50 ATPase Chain: B
Molecule details ›
Chain: B
Length: 144 amino acids
Theoretical weight: 16.36 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P58301 (Residues: 739-882; Coverage: 16%)
Gene names: PF1167, rad50
Sequence domains: AAA domain, putative AbiEii toxin, Type IV TA system
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 67.541Å b: 67.851Å c: 69.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.219
Expression system: Escherichia coli BL21