4L2H
Structure of a catalytically inactive PARG in complex with a poly-ADP-ribose fragment
Summary for 4L2H
Entry DOI | 10.2210/pdb4l2h/pdb |
Descriptor | Poly(ADP-ribose) glycohydrolase, [(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 (3 entities in total) |
Functional Keywords | macrodomain, poly-adp-ribose glycohydrolase, poly-adp-ribose, hydrolase |
Biological source | Tetrahymena thermophila |
Total number of polymer chains | 1 |
Total formula weight | 57003.67 |
Authors | Brassington, A.,Dunstan, M.S.,Leys, D. (deposition date: 2013-06-04, release date: 2013-07-24, Last modification date: 2023-09-20) |
Primary citation | Barkauskaite, E.,Brassington, A.,Tan, E.S.,Warwicker, J.,Dunstan, M.S.,Banos, B.,Lafite, P.,Ahel, M.,Mitchison, T.J.,Ahel, I.,Leys, D. Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities. Nat Commun, 4:2164-2164, 2013 Cited by PubMed: 23917065DOI: 10.1038/ncomms3164 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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