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TitleMINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.
Journal, issue, pagesMol. Cell, Vol. 63, Page 146-155, Year 2016
Publish dateApr 26, 2016 (structure data deposition date)
AuthorsAbdul Rehman, S.A. / Kristariyanto, Y.A. / Choi, S.Y. / Nkosi, P.J. / Weidlich, S. / Labib, K. / Hofmann, K. / Kulathu, Y.
External linksMol. Cell / PubMed:27292798
MethodsX-ray diffraction
Resolution2.65 - 3 Å
Structure data

PDB-5jkn:
Crystal structure of deubiquitinase MINDY-1
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-5jqs:
Crystal structure of deubiquitinase MINDY-1 in complex with Ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HG:
Unknown entry

ChemComp-AYE:
prop-2-en-1-amine

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • bos taurus (domestic cattle)
KeywordsHYDROLASE / Cysteine protease / isopeptidase and Ubiquitin binding

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