› 3uel

X-ray diffraction
3Å resolution

Crystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase bound to ADP-HPD

Released:
DOI: 10.2210/pdb3uel/pdb
PDB entry 3uel coloured by chain, front view.
PDB entry 3uel coloured by chain, side view.
PDB entry 3uel coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.
Kim IK, Kiefer JR, Ho CM, Stegeman RA, Classen S, Tainer JA, Ellenberger T
Nat Struct Mol Biol 19 653-6 (2012)
PMID: 22609859

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-193054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(ADP-ribose) glycohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 588 amino acids
Theoretical weight: 67.78 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9QYM2 (Residues: 385-972; Coverage: 61%)
Gene name: Parg
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand A1R 3 x A1R
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: C2221
Unit cell:
a: 130.773Å b: 195.989Å c: 163.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.246 0.274
Expression system: Escherichia coli

Quick links

Citations

18 review citations

PARP and PARG inhibitors in cancer treatment.
Slade D. (2020)
17 more

3 mentions without citation

Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.
Kim et al. (2012)
2 more