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

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Ligands and binding sites

• AR6 · [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methyl [hydroxy-[[(2R,3S,4R,5S)-3,4,5-trihydroxyoxolan-2-yl]methoxy]phosphoryl] hydrogen phosphate · ligand · 2 copies · chains A
• DTV · (2S,3S)-1,4-dimercaptobutane-2,3-diol · ligand · chains A
• SO4 · Sulfate ion · ion · 2 copies · chains A
• GOL · Glycerol · additive · 2 copies · chains A
• BME · Beta-mercaptoethanol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 2 covalent, 1 modified (additive adduct, covalent ligand, oxidation).

Compared structures

• 4B1H · Structure of human PARG catalytic domain in complex with ADP-ribose · the same entry in another collection · chain A against A, TM-score 1.00
• Q86W56 · AlphaFold monomer V2.0 prediction for POLY(ADP-ribose) glycohydrolase (Q86W56) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q86W56
• Elsewhere: RCSB PDB 4B1H · PDBe 4B1H · UniProt Q86W56