3o3h

X-ray diffraction
2.8Å resolution

T. maritima RNase H2 D107N in complex with nucleic acid substrate and manganese ions

Released:

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-113135 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
1 distinct DNA/RNA hybrid molecule
Macromolecules (3 distinct):
Ribonuclease HII Chain: A
Molecule details ›
Chain: A
Length: 222 amino acids
Theoretical weight: 24.68 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X017 (Residues: 2-223; Coverage: 93%)
Gene names: TM_0915, rnhB
Sequence domains: Ribonuclease HII
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
DNA (5'-D(*GP*AP*AP*TP*CP*AP*GP*GP*TP*GP*TP*C)-3') Chain: C
Molecule details ›
Chain: C
Length: 12 nucleotides
Theoretical weight: 3.7 KDa
Source organism: Thermotoga maritima
Expression system: Not provided
DNA/RNA (5'-D(*GP*AP*CP*AP*C)-R(P*C)-D(P*TP*GP*AP*TP*TP*C)-3') Chain: D
Molecule details ›
Chain: D
Length: 12 nucleotides
Theoretical weight: 3.64 KDa
Source organism: Thermotoga maritima
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 104.658Å b: 48.571Å c: 77.91Å
α: 90° β: 131.97° γ: 90°
R-values:
R R work R free
0.189 0.182 0.253
Expression systems:
  • Escherichia coli
  • Not provided