X-ray diffraction
1.18Å resolution

High Resolution HIV-2 Protease Structure in Complex with Antiviral Inhibitor GRL-98065


Function and Biology Details

Reactions catalysed:
Endopeptidase for which the P1 residue is preferably hydrophobic.
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 99 amino acids
Theoretical weight: 10.73 KDa
Source organism: Human immunodeficiency virus type 2 (ISOLATE ROD)
Expression system: Escherichia coli
  • Canonical: P04584 (Residues: 514-612; Coverage: 7%)
Gene name: gag-pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 105.396Å b: 30.964Å c: 55.625Å
α: 90° β: 91.39° γ: 90°
R R work R free
0.145 0.142 0.188
Expression system: Escherichia coli