4LCD
Structure of an Rsp5xUbxSna3 complex: Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
Summary for 4LCD
Entry DOI | 10.2210/pdb4lcd/pdb |
Descriptor | E3 ubiquitin-protein ligase RSP5, Protein SNA3, Ubiquitin (3 entities in total) |
Functional Keywords | ligase, e3, rsp5, nedd4, ubiquitin, hect, sna3, thioester, maleimide, crosslink, ligase-protein binding complex, ligase/protein binding |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Cellular location | Cytoplasm: P39940 Membrane; Multi-pass membrane protein: P14359 Ubiquitin: Cytoplasm (By similarity): P0CG48 |
Total number of polymer chains | 6 |
Total formula weight | 125228.63 |
Authors | Kamadurai, H.B.,Miller, D.,Schulman, B.A. (deposition date: 2013-06-21, release date: 2013-08-14, Last modification date: 2024-02-28) |
Primary citation | Kamadurai, H.B.,Qiu, Y.,Deng, A.,Harrison, J.S.,Macdonald, C.,Actis, M.,Rodrigues, P.,Miller, D.J.,Souphron, J.,Lewis, S.M.,Kurinov, I.,Fujii, N.,Hammel, M.,Piper, R.,Kuhlman, B.,Schulman, B.A. Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3. Elife, 2:e00828-e00828, 2013 Cited by PubMed: 23936628DOI: 10.7554/eLife.00828 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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