Function and Biology Details
Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Protease/Reverse transcriptase (preferred)
PDBe Complex ID:
PDB-CPX-149873 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease/Reverse transcriptase
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 12.41 KDa
Source organism: Macaque simian foamy virus
Expression system: Escherichia coli
UniProt:
Sequence domains: Spumavirus aspartic protease (A9)
Structure domains: Acid Proteases
Length: 107 amino acids
Theoretical weight: 12.41 KDa
Source organism: Macaque simian foamy virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P23074 (Residues: 1-101; Coverage: 9%)
Sequence domains: Spumavirus aspartic protease (A9)
Structure domains: Acid Proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
simulated annealing
Expression system: Escherichia coli
