› 4fc2

X-ray diffraction
1.91Å resolution

Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain

Released:
DOI: 10.2210/pdb4fc2/pdb
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Source organism: Mus musculus
Primary publication:
Crystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolase.
Wang Z, Gagné JP, Poirier GG, Xu W
OpenAccess logo PLoS One 9 e86010 (2014)
PMID: 24465839

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:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(ADP-ribose) glycohydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 521 amino acids
Theoretical weight: 60.51 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O88622 (Residues: 439-959; Coverage: 54%)
Gene name: Parg
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 28 x SO4
1 modified residue:
Ligand MSE 36 x MSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P1
Unit cell:
a: 67.141Å b: 90.401Å c: 104.696Å
α: 81.64° β: 88.41° γ: 89.36°
R-values:
R R work R free
0.176 0.174 0.214
Expression system: Escherichia coli

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Citations

6 review citations

Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation.
Barkauskaite et al. (2015)
5 more

4 mentions without citation

Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives.
Tucker et al. (2012)
3 more

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