› 5a7r

X-ray diffraction
1.95Å resolution

Human poly(ADP-ribose) glycohydrolase in complex with synthetic dimeric ADP-ribose

Released:
DOI: 10.2210/pdb5a7r/pdb
PDB entry 5a7r coloured by chain, front view.
PDB entry 5a7r coloured by chain, side view.
PDB entry 5a7r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis of dimeric ADP-ribose and its structure with human poly(ADP-ribose) glycohydrolase.
Lambrecht MJ, Brichacek M, Barkauskaite E, Ariza A, Ahel I, Hergenrother PJ
J Am Chem Soc 137 3558-64 (2015)
PMID: 25706250

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: 60.93 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 AR6 2 x AR6
Ligand BME 1 x BME
Ligand SO4 7 x SO4
Ligand GOL 11 x GOL
Ligand PPI 6 x PPI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 67.457Å b: 91.277Å c: 96.123Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.137 0.179
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Macrodomains: Structure, Function, Evolution, and Catalytic Activities.
Rack et al. (2016)
12 more

7 mentions without citation

(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
Rack et al. (2018)
6 more