2LXP
NMR structure of two domains in ubiquitin ligase gp78, RING and G2BR, bound to its conjugating enzyme Ube2g
Summary for 2LXP
Entry DOI | 10.2210/pdb2lxp/pdb |
NMR Information | BMRB: 18688 |
Descriptor | Ubiquitin-conjugating enzyme E2 G2, E3 ubiquitin-protein ligase AMFR, ZINC ION, ... (4 entities in total) |
Functional Keywords | ring domain, ubiquitin, ligase |
Biological source | Homo sapiens (human) More |
Cellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein: Q9UKV5 Q9UKV5 |
Total number of polymer chains | 3 |
Total formula weight | 28421.15 |
Authors | 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: 2024-05-15) |
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 Cited by PubMed: 23942235DOI: 10.1038/emboj.2013.174 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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