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X-ray diffraction
2Å resolution

Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-186355 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chromosome partition protein Smc Chain: X
Molecule details ›
Chain: X
Length: 182 amino acids
Theoretical weight: 20.23 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TZY2 (Residues: 1-182; Coverage: 16%)
Gene names: PF1843, smc
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Chromosome partition protein Smc Chain: Y
Molecule details ›
Chain: Y
Length: 172 amino acids
Theoretical weight: 19.18 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TZY2 (Residues: 1006-1177; Coverage: 15%)
Gene names: PF1843, smc
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: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 102.285Å b: 56.744Å c: 78.869Å
α: 90° β: 123.05° γ: 90°
R-values:
R R work R free
0.207 0.207 0.261
Expression system: Escherichia coli