NMR structure of two domains in ubiquitin ligase gp78, RING and G2BR, bound to its conjugating enzyme Ube2g

Summary for 2LXP

DescriptorUbiquitin-conjugating enzyme E2 G2, E3 ubiquitin-protein ligase AMFR, ZINC ION, ... (4 entities in total)
Functional Keywordsring domain, ubiquitin, ligase
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum membrane; Multi-pass membrane protein Q9UKV5 Q9UKV5
Total number of polymer chains3
Total molecular weight28421.15
Das, R.,Linag, Y.,Mariano, J.,Li, J.,Huang, T.,King, A.,Weissman, A.,Ji, X.,Byrd, R. (deposition date: 2012-08-30, release date: 2013-08-28, Last modification date: 2013-10-02)
Primary citation
Das, R.,Liang, Y.H.,Mariano, J.,Li, J.,Huang, T.,King, A.,Tarasov, S.G.,Weissman, A.M.,Ji, X.,Byrd, R.A.
Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine.
Embo J., 32:2504-2516, 2013
PubMed: 23942235 (PDB entries with the same primary citation)
DOI: 10.1038/emboj.2013.174
MImport into Mendeley
Experimental method
NMR Information

Structure validation

ClashscoreRamachandran outliersSidechain outliers6 0.3% 11.7%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures
Download full validation reportDownload
PDB entries from 2020-12-02