2hah

X-ray diffraction
1.7Å resolution

The structure of FIV 12S protease in complex with TL-3

Released:
Entry authors: Heaslet H, Lin YC, Elder JH, Stout CD

Function and Biology Details

Reactions catalysed:
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.
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
POL protein Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 13.23 KDa
Source organism: Feline immunodeficiency virus (isolate Petaluma)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q66972 (Residues: 39-154; Coverage: 10%)
Gene name: POL
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P3121
Unit cell:
a: 50.324Å b: 50.324Å c: 74.161Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.233
Expression system: Escherichia coli