PDBe 1i4s

X-ray diffraction
2.15Å resolution

CRYSTAL STRUCTURE OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.15 ANGSTROM RESOLUTION

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 147 amino acids
Theoretical weight: 17.28 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67082 (Residues: 1-147; Coverage: 67%)
Gene names: aq_946, rnc
Sequence domains: Ribonuclease III domain
Structure domains: Ribonuclease iii, N-terminal Endonuclease Domain; Chain A

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P212121
Unit cell:
a: 46.157Å b: 51.188Å c: 123.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.212 0.275
Expression system: Escherichia coli