X-ray diffraction
2.8Å resolution

Crystal Structure of C-terminal domain of mouse eRF1 in complex with RNase H domain of RT of Moloney Murine Leukemia Virus


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:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Reverse transcriptase/ribonuclease H Chain: A
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
  • Canonical: P03355 (Residues: 1159-1330; Coverage: 10%)
Gene name: gag-pol
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Eukaryotic peptide chain release factor subunit 1 Chain: B
Molecule details ›
Chain: B
Length: 162 amino acids
Theoretical weight: 18.78 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
  • Canonical: Q8BWY3 (Residues: 276-437; Coverage: 37%)
Gene name: Etf1
Sequence domains: eRF1 domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 89.63Å b: 63.862Å c: 60.431Å
α: 90° β: 96.9° γ: 90°
R R work R free
0.211 0.207 0.28
Expression system: Escherichia coli