2qkk

X-ray diffraction
3.2Å resolution

Human RNase H catalytic domain mutant D210N in complex with 14-mer RNA/DNA hybrid

Released:

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero trimer
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
1 distinct RNA molecule
Macromolecules (3 distinct):
Ribonuclease H1 Chains: A, B, E, F, I, J, M, N, R, S, W
Molecule details ›
Chains: A, B, E, F, I, J, M, N, R, S, W
Length: 154 amino acids
Theoretical weight: 17.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O60930 (Residues: 136-286; Coverage: 53%)
Gene names: RNASEH1, RNH1
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
5'-D(*GP*GP*AP*AP*TP*CP*AP*GP*GP*TP*GP*TP*CP*G)-3' Chains: D, H, L, P, U, Z
Molecule details ›
Chains: D, H, L, P, U, Z
Length: 14 nucleotides
Theoretical weight: 4.36 KDa
Source organism: Homo sapiens
Expression system: Not provided
5'-R(*CP*GP*AP*CP*AP*CP*CP*UP*GP*AP*UP*UP*CP*C)-3' Chains: C, G, K, O, T, X
Molecule details ›
Chains: C, G, K, O, T, X
Length: 14 nucleotides
Theoretical weight: 4.38 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 151.065Å b: 176.2Å c: 125.845Å
α: 90° β: 90.22° γ: 90°
R-values:
R R work R free
0.212 0.212 0.268
Expression systems:
  • Escherichia coli BL21
  • Not provided