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TitleChemical Protein Synthesis Enabled Mechanistic Studies on the Molecular Recognition of K27-linked Ubiquitin Chains.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 58, Page 2627-2631, Year 2019
Publish dateNov 19, 2018 (structure data deposition date)
AuthorsPan, M. / Zheng, Q. / Ding, S. / Zhang, L. / Qu, Q. / Wang, T. / Hong, D. / Ren, Y. / Liang, L. / Chen, C. ...Pan, M. / Zheng, Q. / Ding, S. / Zhang, L. / Qu, Q. / Wang, T. / Hong, D. / Ren, Y. / Liang, L. / Chen, C. / Mei, Z. / Liu, L.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:30589182
MethodsX-ray diffraction
Resolution1.866 Å
Structure data

PDB-6isu:
Crystal structure of Lys27-linked di-ubiquitin in complex with its selective interacting protein UCHL3
Method: X-RAY DIFFRACTION / Resolution: 1.866 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Ubiquitination / UCHL3 / Lys27-linked di-ubiquitin

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