PDBe 2abk

X-ray diffraction
1.85Å resolution

REFINEMENT OF THE NATIVE STRUCTURE OF ENDONUCLEASE III TO A RESOLUTION OF 1.85 ANGSTROM

Released:

Function and Biology Details

Reaction catalysed:
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endonuclease III Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 23.6 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0AB83 (Residues: 1-211; Coverage: 100%)
Gene names: JW1625, b1633, nth
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 48.5Å b: 65.8Å c: 86.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.216