2x6s

X-ray diffraction
2.29Å resolution

Human foamy virus integrase - catalytic core. Magnesium-bound structure.

Released:
Source organism: Human spumaretrovirus
Primary publication:
Structural studies of the catalytic core of the primate foamy virus (PFV-1) integrase.
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 881-6 (2010)
PMID: 20693659

Function and Biology Details

Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Integrase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 200 amino acids
Theoretical weight: 22.58 KDa
Source organism: Human spumaretrovirus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14350 (Residues: 861-1060; Coverage: 18%)
Gene name: pol
Sequence domains: Integrase core domain
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 84.35Å b: 89.19Å c: 177.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.225 0.278
Expression system: Escherichia coli BL21(DE3)