› 1ril

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF RIBONUCLEASE H FROM THERMUS THERMOPHILUS HB8 REFINED AT 2.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1ril/pdb
PDB entry 1ril coloured by chain, front view.
PDB entry 1ril coloured by chain, side view.
PDB entry 1ril coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 A resolution.
Ishikawa K, Okumura M, Katayanagi K, Kimura S, Kanaya S, Nakamura H, Morikawa K
J Mol Biol 230 529-42 (1993)
PMID: 8385228

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151372 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease H Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.76 KDa
Source organism: Thermus thermophilus
Expression system: Not provided
UniProt:
  • Canonical: P29253 (Residues: 1-166; Coverage: 100%)
Gene names: TTHA1556, 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
Spacegroup: P6522
Unit cell:
a: 44.7Å b: 44.7Å c: 314.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 not available not available
Expression system: Not provided

Quick links

Citations

9 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
8 more

23 mentions without citation

Enzyme dynamics from NMR spectroscopy.
Palmer AG. (2015)
22 more