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Structure paper

TitleThe entropic force generated by intrinsically disordered segments tunes protein function.
Journal, issue, pagesNature, Vol. 563, Page 584-588, Year 2018
Publish dateMay 10, 2017 (structure data deposition date)
AuthorsKeul, N.D. / Oruganty, K. / Schaper Bergman, E.T. / Beattie, N.R. / McDonald, W.E. / Kadirvelraj, R. / Gross, M.L. / Phillips, R.S. / Harvey, S.C. / Wood, Z.A.
External linksNature / PubMed:30420606
MethodsX-ray diffraction
Resolution1.999 - 2.65 Å
Structure data

PDB-5vr8:
Human UDP-Glucose Dehydrogenase with UDP-Xylose Bound to the Co-enzyme Site
Method: X-RAY DIFFRACTION / Resolution: 1.999 Å

PDB-5w4x:
Truncated hUGDH
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-UDX:
URIDINE-5'-DIPHOSPHATE-XYLOPYRANOSE

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-PG5:
1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / hUGDH / UDP-Xylose / UDX / UDP-Glucose dehydrogenase / DEHYDROGENASE / UDP-SUGAR BINDING / UDP-GLUCURONIC ACID / ROSSMANN FOLD / OXIDATION / CYTOSOL

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