2e4l

X-ray diffraction
2Å resolution

Thermodynamic and Structural Analysis of Thermolabile RNase HI from Shewanella oneidensis MR-1

Released:
Model geometry
Fit model/data

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HI Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.81 KDa
Source organism: Shewanella oneidensis MR-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EE30 (Residues: 1-158; Coverage: 100%)
Gene names: SO_2560, rnhA
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P422
Unit cell:
a: 77.128Å b: 77.128Å c: 76.661Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.219
Expression system: Escherichia coli