3ogp

X-ray diffraction
1.7Å resolution

Crystal Structure of 6s-98S FIV Protease with Darunavir bound

Released:

Function and Biology Details

Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
dUTP + H(2)O = dUMP + diphosphate
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
Macromolecule:
Protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 116 amino acids
Theoretical weight: 13.23 KDa
Source organism: Feline immunodeficiency virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16088 (Residues: 39-154; Coverage: 10%)
Gene name: pol
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 BL11-1
Spacegroup: P31
Unit cell:
a: 81.17Å b: 81.17Å c: 33.59Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.185 0.229
Expression system: Escherichia coli BL21(DE3)