4epp

X-ray diffraction
1.95Å resolution

Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.

Released:

Function and Biology Details

Reaction catalysed:
Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(ADP-ribose) glycohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 477 amino acids
Theoretical weight: 55.89 KDa
Source organism: Tetrahymena thermophila
Expression system: Escherichia coli
UniProt:
  • Canonical: I6L8L8 (Residues: 1-457; Coverage: 100%)
Sequence domains: Poly (ADP-ribose) glycohydrolase (PARG)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P41
Unit cell:
a: 112.7Å b: 112.7Å c: 88.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.207
Expression system: Escherichia coli