4LAD
Crystal Structure of the Ube2g2:RING-G2BR complex
Summary for 4LAD
Entry DOI | 10.2210/pdb4lad/pdb |
Related | 2LXH 2LXP |
Descriptor | Ubiquitin-conjugating enzyme E2 G2, E3 ubiquitin-protein ligase AMFR, ZINC ION, ... (5 entities in total) |
Functional Keywords | e2:e3 complex, ligase-ligase complex, ligase/ligase |
Biological source | Homo sapiens (human) More |
Cellular location | Endoplasmic reticulum membrane ; Multi-pass membrane protein : Q9UKV5 |
Total number of polymer chains | 2 |
Total formula weight | 34360.18 |
Authors | Liang, Y.-H.,Li, J.,Das, R.,Byrd, R.A.,Ji, X. (deposition date: 2013-06-19, release date: 2013-08-28, Last modification date: 2023-09-20) |
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 | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report