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Structure paper

TitleE2 enzyme inhibition by stabilization of a low-affinity interface with ubiquitin.
Journal, issue, pagesNat. Chem. Biol., Vol. 10, Page 156-163, Year 2014
Publish dateAug 22, 2013 (structure data deposition date)
AuthorsHuang, H. / Ceccarelli, D.F. / Orlicky, S. / St-Cyr, D.J. / Ziemba, A. / Garg, P. / Plamondon, S. / Auer, M. / Sidhu, S. / Marinier, A. ...Huang, H. / Ceccarelli, D.F. / Orlicky, S. / St-Cyr, D.J. / Ziemba, A. / Garg, P. / Plamondon, S. / Auer, M. / Sidhu, S. / Marinier, A. / Kleiger, G. / Tyers, M. / Sicheri, F.
External linksNat. Chem. Biol. / PubMed:24316736
MethodsX-ray diffraction
Resolution2.6095 Å
Structure data

PDB-4mdk:
Cdc34-ubiquitin-CC0651 complex
Method: X-RAY DIFFRACTION / Resolution: 2.6095 Å

Chemicals

ChemComp-U94:
4,5-dideoxy-5-(3',5'-dichlorobiphenyl-4-yl)-4-[(methoxyacetyl)amino]-L-arabinonic acid

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE/LIGASE INHIBITOR / ubiquitin conjugating enzyme domain / E2 ligase inhibitor / LIGASE-LIGASE INHIBITOR complex

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