› 1rnh

X-ray diffraction
2Å resolution

STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN

Released:
DOI: 10.2210/pdb1rnh/pdb
PDB entry 1rnh coloured by chain, front view.
PDB entry 1rnh coloured by chain, side view.
PDB entry 1rnh coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein.
Yang W, Hendrickson WA, Crouch RJ, Satow Y
Science 249 1398-405 (1990)
PMID: 2169648

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-141635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HI Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.81 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7Y4 (Residues: 1-155; Coverage: 100%)
Gene names: JW0204, b0214, dasF, herA, rnh, rnhA, sdrA
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 41.79Å b: 86.34Å c: 36.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 not available not available
Expression system: Escherichia coli

Quick links

Citations

51 review citations

Adding new chemistries to the genetic code.
Liu et al. (2010)
50 more

12 mentions without citation

Structural studies of DNA end detection and resection in homologous recombination.
Schiller et al. (2014)
11 more