› 4b1j

X-ray diffraction
2.08Å resolution

Structure of human PARG catalytic domain in complex with ADP-HPD

Released:
DOI: 10.2210/pdb4b1j/pdb
PDB entry 4b1j coloured by chain, front view.
PDB entry 4b1j coloured by chain, side view.
PDB entry 4b1j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives.
Tucker JA, Bennett N, Brassington C, Durant ST, Hassall G, Holdgate G, McAlister M, Nissink JW, Truman C, Watson M
PLoS One 7 e50889 (2012)
PMID: 23251397

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-183229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(ADP-ribose) glycohydrolase Chain: A
Molecule details ›
Chain: A
Length: 531 amino acids
Theoretical weight: 60.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86W56 (Residues: 448-976; Coverage: 54%)
Gene name: PARG
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand A1R 1 x A1R
Ligand SO4 3 x SO4
1 modified residue:
Ligand CSS 1 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P212121
Unit cell:
a: 66.848Å b: 90.971Å c: 94.763Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.215
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

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

4 mentions without citation

Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation.
Feijs et al. (2013)
3 more