Function and Biology Details
Reactions catalysed:
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.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
PROTEIN (SIV INTEGRASE) (preferred)
PDBe Complex ID:
PDB-CPX-183402 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UNLIGANDED SIV PROTEASE
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.79 KDa
Source organism: Simian immunodeficiency virus
Expression system: Not provided
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.79 KDa
Source organism: Simian immunodeficiency virus
Expression system: Not provided
UniProt:
- Canonical:
Q88016 (Residues: 110-208; Coverage: 9%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
C2221
Expression system: Not provided
