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Structure paper

TitleCrystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme.
Journal, issue, pagesFebs J., Vol. 278, Page 4917-4926, Year 2011
Publish dateApr 13, 2011 (structure data deposition date)
AuthorsMaiti, T.K. / Permaul, M. / Boudreaux, D.A. / Mahanic, C. / Mauney, S. / Das, C.
External linksFebs J. / PubMed:21995438
MethodsX-ray diffraction
Resolution2.0008 - 2.398 Å
Structure data

PDB-3rii:
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme
Method: X-RAY DIFFRACTION / Resolution: 2.0008 Å

PDB-3ris:
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme
Method: X-RAY DIFFRACTION / Resolution: 2.398 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
KeywordsHYDROLASE / alpha-beta-alpha fold / Thiol hydroalse / Cysteine protease / deubiquitinating enzyme / ubiquitin hydrolase / thiol hydrolase

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