1fiv

X-ray diffraction
2Å resolution

STRUCTURE OF AN INHIBITOR COMPLEX OF PROTEINASE FROM FELINE IMMUNODEFICIENCY VIRUS

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:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protease Chain: A
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 12.84 KDa
Source organism: Feline immunodeficiency virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P16088 (Residues: 42-154; Coverage: 10%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
FIV PROTEASE INHIBITOR ACE-ALN-VAL-STA-GLU-ALN-NH2 Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 822 Da
Source organism: Feline immunodeficiency virus
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 50.65Å b: 50.65Å c: 74.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.148 0.148 not available
Expression systems:
  • Escherichia coli
  • Not provided