4LCD

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

Summary for 4LCD

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 molecular weight125228.63
Authors
Kamadurai, H.B.,Miller, D.,Schulman, B.A. (deposition date: 2013-06-21, release date: 2013-08-14, Last modification date: 2013-08-28)
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
PubMed: 23936628 (PDB entries with the same primary citation)
DOI: 10.7554/eLife.00828
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3.1 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.299150.1%8.2%2.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report