7AOM
Structure of NUDT15 in complex with Ganciclovir triphosphate
Summary for 7AOM
Entry DOI | 10.2210/pdb7aom/pdb |
Descriptor | Nucleotide triphosphate diphosphatase NUDT15, Ganciclovir triphosphate, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | nudix hydrolase, antiviral, hydrolase |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 2 |
Total formula weight | 38308.95 |
Authors | Rehling, D.,Zhang, S.M.,Helleday, T.,Stenmark, P. (deposition date: 2020-10-14, release date: 2021-06-02, Last modification date: 2024-01-31) |
Primary citation | Zhang, S.M.,Rehling, D.,Jemth, A.S.,Throup, A.,Landazuri, N.,Almlof, I.,Gottmann, M.,Valerie, N.C.K.,Borhade, S.R.,Wakchaure, P.,Page, B.D.G.,Desroses, M.,Homan, E.J.,Scobie, M.,Rudd, S.G.,Berglund, U.W.,Soderberg-Naucler, C.,Stenmark, P.,Helleday, T. NUDT15-mediated hydrolysis limits the efficacy of anti-HCMV drug ganciclovir. Cell Chem Biol, 28:1693-1702.e6, 2021 Cited by PubMed: 34192523DOI: 10.1016/j.chembiol.2021.06.001 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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