› 4n9z

X-ray diffraction
1.9Å resolution

Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain mutant E749Q

Released:
DOI: 10.2210/pdb4n9z/pdb
PDB entry 4n9z coloured by chain, front view.
PDB entry 4n9z coloured by chain, side view.
PDB entry 4n9z 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 Chains: A, B
Molecule details ›
Chains: A, B
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 V3L 2 x V3L
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 66.915Å b: 91.283Å c: 102.522Å
α: 90° β: 91.2° γ: 90°
R-values:
R R work R free
0.192 0.19 0.23
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)