X-ray diffraction
1.4Å resolution

Apo Wild-type HIV Protease in the open conformation

Primary publication:
Conformational flexibility in the flap domains of ligand-free HIV protease.
Acta Crystallogr. D Biol. Crystallogr. 63 866-75 (2007)
PMID: 17642513

Function and Biology Details

Reaction catalysed:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
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: 99 amino acids
Theoretical weight: 10.83 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
  • Canonical: Q903N5 (Residues: 1-99; Coverage: 100%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P41212
Unit cell:
a: 46.416Å b: 46.416Å c: 101.37Å
α: 90° β: 90° γ: 90°
R R work R free
0.155 0.153 0.186
Expression system: Escherichia coli