› 3p5j

X-ray diffraction
2.9Å resolution

The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease

Released:
DOI: 10.2210/pdb3p5j/pdb
PDB entry 3p5j coloured by chain, front view.
PDB entry 3p5j coloured by chain, side view.
PDB entry 3p5j coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease.
Reijns MA, Bubeck D, Gibson LC, Graham SC, Baillie GS, Jones EY, Jackson AP
OpenAccess logo J Biol Chem 286 10530-9 (2011)
PMID: 21177854

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182412 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ribonuclease H2 subunit A Chain: A
Molecule details ›
Chain: A
Length: 301 amino acids
Theoretical weight: 33.55 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9CWY8 (Residues: 1-301; Coverage: 100%)
Gene names: Rnaseh2a, Rnasehi
Sequence domains: Ribonuclease HII
Structure domains:
Ribonuclease H2 subunit B Chain: B
Molecule details ›
Chain: B
Length: 332 amino acids
Theoretical weight: 37.49 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q80ZV0 (Residues: 1-308; Coverage: 100%)
Gene names: Dleu8, Rnaseh2b
Sequence domains:
Structure domains:
Ribonuclease H2 subunit C Chain: C
Molecule details ›
Chain: C
Length: 166 amino acids
Theoretical weight: 17.85 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9CQ18 (Residues: 1-166; Coverage: 100%)
Gene names: Ayp1, Rnaseh2c
Sequence domains: Ribonuclease H2 non-catalytic subunit (Ylr154p-like)
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 279.29Å b: 40.42Å c: 67.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.21 0.272
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Processing ribonucleotides incorporated during eukaryotic DNA replication.
Williams et al. (2016)
8 more

2 mentions without citation

The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease.
Reijns et al. (2011)
1 more