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4LCD

Structure of an Rsp5xUbxSna3 complex: Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3

Summary for 4LCD
Entry DOI10.2210/pdb4lcd/pdb
DescriptorE3 ubiquitin-protein ligase RSP5, Protein SNA3, Ubiquitin (3 entities in total)
Functional Keywordsligase, e3, rsp5, nedd4, ubiquitin, hect, sna3, thioester, maleimide, crosslink, ligase-protein binding complex, ligase/protein binding
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
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Cellular locationCytoplasm: P39940
Membrane; Multi-pass membrane protein: P14359
Ubiquitin: Cytoplasm (By similarity): P0CG48
Total number of polymer chains6
Total formula weight125228.63
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 citationKamadurai, 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: 23936628
DOI: 10.7554/eLife.00828
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

217705

数据于2024-03-27公开中

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