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Structure paper

TitleThe structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 17362-17374, Year 2018
Publish dateMay 6, 2018 (structure data deposition date)
AuthorsWard, S.J. / Gratton, H.E. / Indrayudha, P. / Michavila, C. / Mukhopadhyay, R. / Maurer, S.K. / Caulton, S.G. / Emsley, J. / Dreveny, I.
External linksJ. Biol. Chem. / PubMed:30228188
MethodsX-ray diffraction
Resolution1.98 - 2.09 Å
Structure data

PDB-6gh9:
USP15 catalytic domain in complex with small molecule
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-6gha:
USP15 catalytic domain structure
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-MIX:
1,4-DIHYDROXY-5,8-BIS({2-[(2-HYDROXYETHYL)AMINO]ETHYL}AMINO)-9,10-ANTHRACENEDIONE / antineoplastic*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / protease / ubiquitin / ubiquitin specific protease / inhibitor / mitoxantrone

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