8UQA
Crystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 12-residue linker
Summary for 8UQA
Entry DOI | 10.2210/pdb8uqa/pdb |
Descriptor | E3 ubiquitin-protein ligase RNF168,Ubiquitin-conjugating enzyme E2 D3,Histone H2B type 2-E,Histone H2A type 1-B/E, SODIUM ION, ZINC ION, ... (5 entities in total) |
Functional Keywords | rnf168, ubch5c, histone h2a, histone h2b, chromatin, ubiquitin ligase, ubiquitin-conjugating enzyme, dna damage response, dna double-strand break repair, protein binding, protein binding-transferase complex, transferase |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 1 |
Total formula weight | 49865.46 |
Authors | Hu, Q.,Botuyan, M.V.,Mer, G. (deposition date: 2023-10-23, release date: 2024-01-17, Last modification date: 2024-03-20) |
Primary citation | Hu, Q.,Zhao, D.,Cui, G.,Bhandari, J.,Thompson, J.R.,Botuyan, M.V.,Mer, G. Mechanisms of RNF168 nucleosome recognition and ubiquitylation. Mol.Cell, 84:839-853.e12, 2024 Cited by PubMed: 38242129DOI: 10.1016/j.molcel.2023.12.036 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.049 Å) |
Structure validation
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