Function and Biology Details
Reactions catalysed:
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.
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
- not assigned
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-210531 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Capsid protein p24
Molecule details ›
Chains: A, B
Length: 151 amino acids
Theoretical weight: 16.72 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Human Immunodeficiency Virus Type 1 Capsid Protein
Length: 151 amino acids
Theoretical weight: 16.72 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P12497 (Residues: 133-283; Coverage: 11%)
Structure domains: Human Immunodeficiency Virus Type 1 Capsid Protein
Ig-like domain-containing protein
Molecule details ›
Chains: H, K
Length: 220 amino acids
Theoretical weight: 23.7 KDa
Source organism: Mus musculus
UniProt:
Sequence domains:
Structure domains: Immunoglobulins
Length: 220 amino acids
Theoretical weight: 23.7 KDa
Source organism: Mus musculus
UniProt:
- Canonical: Q99LC4 (Residues: 20-239; Coverage: 50%)
Sequence domains:
Structure domains: Immunoglobulins
