3w0f

X-ray diffraction
2Å resolution

Crystal structure of mouse Endonuclease VIII-LIKE 3 (mNEIL3)

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
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185056 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endonuclease 8-like 3 Chain: A
Molecule details ›
Chain: A
Length: 287 amino acids
Theoretical weight: 31.85 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8K203 (Residues: 2-282; Coverage: 46%)
Gene name: Neil3
Sequence domains: Formamidopyrimidine-DNA glycosylase H2TH domain
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 115.58Å b: 43.823Å c: 77.645Å
α: 90° β: 128.96° γ: 90°
R-values:
R R work R free
0.201 0.197 0.235
Expression system: Escherichia coli