8P83
Cryo-EM structure of full-length human UBR5 (homotetramer)
Summary for 8P83
Entry DOI | 10.2210/pdb8p83/pdb |
EMDB information | 17540 |
Descriptor | E3 ubiquitin-protein ligase UBR5 (1 entity in total) |
Functional Keywords | e3, ubiquitin ligase, hect, ligase |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 4 |
Total formula weight | 1253054.75 |
Authors | Aguirre, J.D.,Kater, L.,Kempf, G.,Cavadini, S.,Thoma, N.H. (deposition date: 2023-05-31, release date: 2023-06-14, Last modification date: 2023-08-16) |
Primary citation | Tsai, J.M.,Aguirre, J.D.,Li, Y.D.,Brown, J.,Focht, V.,Kater, L.,Kempf, G.,Sandoval, B.,Schmitt, S.,Rutter, J.C.,Galli, P.,Sandate, C.R.,Cutler, J.A.,Zou, C.,Donovan, K.A.,Lumpkin, R.J.,Cavadini, S.,Park, P.M.C.,Sievers, Q.,Hatton, C.,Ener, E.,Regalado, B.D.,Sperling, M.T.,Slabicki, M.,Kim, J.,Zon, R.,Zhang, Z.,Miller, P.G.,Belizaire, R.,Sperling, A.S.,Fischer, E.S.,Irizarry, R.,Armstrong, S.A.,Thoma, N.H.,Ebert, B.L. UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability. Mol.Cell, 83:2753-, 2023 Cited by PubMed: 37478846DOI: 10.1016/j.molcel.2023.06.028 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.87 Å) |
Structure validation
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