X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Protease Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.39 KDa
Source organism: Equine infectious anemia virus
Expression system: Escherichia coli
  • Canonical: Q66729 (Residues: 28-131; Coverage: 50%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: C2
Unit cell:
a: 42.65Å b: 45.36Å c: 56.76Å
α: 90° β: 110.36° γ: 90°
R R work R free
0.143 0.143 not available
Expression system: Escherichia coli