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
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: 172 amino acids
Theoretical weight: 18.77 KDa
Source organism: Moloney murine leukemia virus isolate Shinnick
Expression system: Escherichia coli
UniProt:
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Length: 172 amino acids
Theoretical weight: 18.77 KDa
Source organism: Moloney murine leukemia virus isolate Shinnick
Expression system: Escherichia coli
UniProt:
- Canonical:
P03355 (Residues: 1159-1330; Coverage: 10%)
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Eukaryotic peptide chain release factor subunit 1
Molecule details ›
Chain: B
Length: 162 amino acids
Theoretical weight: 18.78 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: eRF1 domain 3
Length: 162 amino acids
Theoretical weight: 18.78 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: Q8BWY3 (Residues: 276-437; Coverage: 37%)
Sequence domains: eRF1 domain 3
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
DIAMOND BEAMLINE I02
Spacegroup:
C2
Expression system: Escherichia coli
