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: 2023-06-14)

• 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; DOI: 10.1038/emboj.2013.174

Experimental method

SOLUTION NMR