2rpi

Solution NMR

The NMR structure of the submillisecond folding intermediate of the Thermus thermophilus ribonuclease H

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease H Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.88 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: P29253 (Residues: 1-127; Coverage: 64%)
Gene names: TTHA1556, rnhA
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DGSA-distance geometry simulated annealing, torsion angle dynamics
Expression system: Escherichia coli