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TitleE3 ubiquitin-protein ligase TRIM21-mediated lysine capture by UBE2E1 reveals substrate-targeting mode of a ubiquitin-conjugating E2.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 11404-11419, Year 2019
Publish dateJan 10, 2018 (structure data deposition date)
AuthorsAnandapadamanaban, M. / Kyriakidis, N.C. / Csizmok, V. / Wallenhammar, A. / Espinosa, A.C. / Ahlner, A. / Round, A.R. / Trewhella, J. / Moche, M. / Wahren-Herlenius, M. / Sunnerhagen, M.
External linksJ. Biol. Chem. / PubMed:31160341
MethodsX-ray diffraction
Resolution2.82 Å
Structure data

PDB-6fga:
Crystal structure of TRIM21 E3 ligase, RING domain in complex with its cognate E2 conjugating enzyme UBE2E1
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / RING-type E3 ligase / UBC core domain and Ubiquitination

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