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2LXH

NMR structure of the RING domain in ubiquitin ligase gp78

Summary for 2LXH
Entry DOI10.2210/pdb2lxh/pdb
NMR InformationBMRB: 18677
DescriptorE3 ubiquitin-protein ligase AMFR, ZINC ION (2 entities in total)
Functional Keywordsring domain, ubiquitin, ligase
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum membrane; Multi-pass membrane protein: Q9UKV5
Total number of polymer chains1
Total formula weight9372.27
Authors
Das, R.,Linag, Y.,Mariano, J.,Li, J.,Huang, T.,King, A.,Weissman, A.,Ji, X.,Byrd, R. (deposition date: 2012-08-27, release date: 2013-08-28, Last modification date: 2023-06-14)
Primary citationDas, 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: 23942235
DOI: 10.1038/emboj.2013.174
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

217705

數據於2024-03-27公開中

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