Function and Biology Details
Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Reverse transcriptase/ribonuclease H and DNA (preferred)
PDBe Complex ID:
PDB-CPX-114961 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (3 distinct):
Reverse transcriptase/ribonuclease H
Molecule details ›
Chain: A
Length: 255 amino acids
Theoretical weight: 28.93 KDa
Source organism: Moloney murine leukemia virus
Expression system: Escherichia coli
UniProt:
Sequence domains: Reverse transcriptase (RNA-dependent DNA polymerase)
Structure domains:
Length: 255 amino acids
Theoretical weight: 28.93 KDa
Source organism: Moloney murine leukemia virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P03355 (Residues: 683-937; Coverage: 15%)
Sequence domains: Reverse transcriptase (RNA-dependent DNA polymerase)
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-BM
Spacegroup:
P21212
Expression systems:
- Escherichia coli
- Not provided
