3g1k

X-ray diffraction
3.1Å resolution

Mth0212 (WT) crystallized in a monoclinic space group

Released:

Function and Biology Details

Reactions catalysed:
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
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)
PDBe Complex ID:
PDB-CPX-127832 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA uridine endonuclease Chains: A, B
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 31.43 KDa
Source organism: Methanothermobacter thermautotrophicus str. Delta H
Expression system: Escherichia coli
UniProt:
  • Canonical: O26314 (Residues: 1-257; Coverage: 100%)
Gene name: MTH_212
Sequence domains: Endonuclease/Exonuclease/phosphatase family
Structure domains: Endonuclease/exonuclease/phosphatase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 44.635Å b: 80.345Å c: 81.839Å
α: 90° β: 90.32° γ: 90°
R-values:
R R work R free
0.206 0.203 0.266
Expression system: Escherichia coli