4LAD

Crystal Structure of the Ube2g2:RING-G2BR complex

Summary for 4LAD

Related2LXH 2LXP
DescriptorUbiquitin-conjugating enzyme E2 G2, E3 ubiquitin-protein ligase AMFR, ZINC ION, ... (5 entities in total)
Functional Keywordse2:e3 complex, ligase-ligase complex, ligase/ligase
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum membrane ; Multi-pass membrane protein  Q9UKV5
Total number of polymer chains2
Total molecular weight34360.18
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: 2017-11-15)
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
PubMed: 23942235 (PDB entries with the same primary citation)
DOI: 10.1038/emboj.2013.174
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.3 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.26615 1.9% 10.7% 8.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
171916
PDB entries from 2020-12-02