6Y73
The crystal structure of human MACROD2 in space group P43
Summary for 6Y73
| Entry DOI | 10.2210/pdb6y73/pdb |
| Related | 6Y4Y 6Y4Z |
| Descriptor | ADP-ribose glycohydrolase MACROD2, GLYCEROL, L(+)-TARTARIC ACID, ... (5 entities in total) |
| Functional Keywords | adp-ribosylhydrolase, macrodomain, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 8 |
| Total formula weight | 328621.92 |
| Authors | Wazir, S.,Maksimainen, M.M.,Lehtio, L. (deposition date: 2020-02-28, release date: 2020-09-30, Last modification date: 2024-01-24) |
| Primary citation | Wazir, S.,Maksimainen, M.M.,Lehtio, L. Multiple crystal forms of human MacroD2. Acta Crystallogr.,Sect.F, 76:477-482, 2020 Cited by PubMed Abstract: MacroD2 is one of the three human macrodomain proteins characterized by their protein-linked mono-ADP-ribosyl-hydrolyzing activity. MacroD2 is a single-domain protein that contains a deep ADP-ribose-binding groove. In this study, new crystallization conditions for MacroD2 were found and three crystal structures of human MacroD2 in the apo state were solved in space groups P422, P422 and P4, and refined at 1.75, 1.90 and 1.70 Å resolution, respectively. Structural comparison of the apo crystal structures with the previously reported crystal structure of MacroD2 in complex with ADP-ribose revealed conformational changes in the side chains of Val101, Ile189 and Phe224 induced by the binding of ADP-ribose in the active site. These conformational variations may potentially facilitate design efforts of a MacroD2 inhibitor. PubMed: 33006575DOI: 10.1107/S2053230X20011309 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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