3p56

X-ray diffraction
4.06Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131120 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ribonuclease H2 subunit A Chains: A, D
Molecule details ›
Chains: A, D
Length: 299 amino acids
Theoretical weight: 33.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O75792 (Residues: 1-299; Coverage: 100%)
Gene names: RNASEH2A, RNASEHI, RNHIA
Sequence domains: Ribonuclease HII
Ribonuclease H2 subunit B Chains: B, E
Molecule details ›
Chains: B, E
Length: 237 amino acids
Theoretical weight: 26.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q5TBB1 (Residues: 2-226; Coverage: 72%)
Gene names: DLEU8, RNASEH2B
Sequence domains:
Ribonuclease H2 subunit C Chains: C, F
Molecule details ›
Chains: C, F
Length: 164 amino acids
Theoretical weight: 17.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8TDP1 (Residues: 1-164; Coverage: 100%)
Gene names: AYP1, RNASEH2C
Sequence domains: Ribonuclease H2 non-catalytic subunit (Ylr154p-like)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 212.238Å b: 42.302Å c: 186.95Å
α: 90° β: 98.11° γ: 90°
R-values:
R R work R free
0.375 0.374 0.379
Expression system: Escherichia coli BL21