› 4b1h

X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb4b1h/pdb
PDB entry 4b1h coloured by chain, front view.
PDB entry 4b1h coloured by chain, side view.
PDB entry 4b1h 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: 60.96 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

5 bound ligands:
Ligand BME 1 x BME
Ligand DTV 1 x DTV
Ligand GOL 2 x GOL
Ligand AR6 2 x AR6
Ligand SO4 2 x SO4
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P212121
Unit cell:
a: 66.929Å b: 90.656Å c: 94.975Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

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

10 mentions without citation

(ADP-ribosyl)hydrolases: structure, function, and biology.
Rack et al. (2020)
9 more