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:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136826 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Reverse transcriptase/ribonuclease H
Molecule details ›
Chain: A
Length: 648 amino acids
Theoretical weight: 72.14 KDa
Source organism: Moloney murine leukemia virus isolate Shinnick
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 648 amino acids
Theoretical weight: 72.14 KDa
Source organism: Moloney murine leukemia virus isolate Shinnick
Expression system: Escherichia coli
UniProt:
- Canonical:
P03355 (Residues: 683-1330; Coverage: 37%)
Sequence domains:
- Reverse transcriptase (RNA-dependent DNA polymerase)
- RNase H-like domain found in reverse transcriptase
- RNase H
Eukaryotic peptide chain release factor subunit 1
Molecule details ›
Chain: B
Length: 437 amino acids
Theoretical weight: 49.09 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 437 amino acids
Theoretical weight: 49.09 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: Q8BWY3 (Residues: 1-437; Coverage: 100%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SLS BEAMLINE X06SA
Spacegroup:
P3221
Expression system: Escherichia coli
