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Structure paper

TitleDifferential Oligomerization of the Deubiquitinases USP25 and USP28 Regulates Their Activities.
Journal, issue, pagesMol. Cell, Vol. 74, Page 421-, Year 2019
Publish dateJul 21, 2018 (structure data deposition date)
AuthorsSauer, F. / Klemm, T. / Kollampally, R.B. / Tessmer, I. / Nair, R.K. / Popov, N. / Kisker, C.
External linksMol. Cell / PubMed:30926243
MethodsX-ray diffraction
Resolution2.05 - 3.5 Å
Structure data

PDB-6h4h:
Usp28 catalytic domain variant E593D in complex with UbPA
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

PDB-6h4i:
Usp28 catalytic domain apo
Method: X-RAY DIFFRACTION / Resolution: 3.22 Å

PDB-6h4j:
Usp25 catalytic domain
Method: X-RAY DIFFRACTION / Resolution: 3.07 Å

PDB-6h4k:
Structure of the Usp25 C-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-SO4:
SULFATE ION

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

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Ubiquitin / Deubiquitinase / Usp / Cancer / IMMUNE SYSTEM

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