› 4ll3

X-ray diffraction
1.95Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 99 amino acids
Theoretical weight: 10.83 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Not provided
UniProt:
  • Canonical: Q9WFL7 (Residues: 7-105; Coverage: 29%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand 017 2 x 017
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P61
Unit cell:
a: 62.557Å b: 62.557Å c: 81.523Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.183 0.23
Expression system: Not provided

Quick links

Citations

4 review citations

Retroviral proteases and their roles in virion maturation.
Konvalinka et al. (2015)
3 more

20 mentions without citation

Viral proteases as therapeutic targets.
Majerová et al. (2022)
19 more