› 4n9y

X-ray diffraction
2.3Å resolution

Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain mutant E748Q

Released:
DOI: 10.2210/pdb4n9y/pdb
PDB entry 4n9y coloured by chain, front view.
PDB entry 4n9y coloured by chain, side view.
PDB entry 4n9y coloured by chain, top view.
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
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 Chain: A
Molecule details ›
Chain: A
Length: 522 amino acids
Theoretical weight: 60.15 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

2 bound ligands:
Ligand SO4 6 x SO4
Ligand V3L 1 x V3L
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21212
Unit cell:
a: 67.239Å b: 91.103Å c: 102.764Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.24
Expression system: Escherichia coli

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Citations

5 review citations

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

1 mention without citation

Crystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolase.
Wang et al. (2014)