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Structure paper

TitleLys11-Linked Ubiquitin Chains Adopt Compact Conformations and are Preferentially Hydrolyzed by the Deubiquitinase Cezanne
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 17, Page 939-, Year 2010
Publish dateMay 18, 2010 (structure data deposition date)
AuthorsBremm, A. / Freund, S.M.V. / Komander, D.
External linksNat. Struct. Mol. Biol. / PubMed:20622874
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-2xew:
Crystal structure of K11-linked diubiquitin
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-FLC:
CITRATE ANION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / PROTEIN DEGRADATION / PROTEASOME / DEUBIQUITINATION

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