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Structure paper

TitleEngineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins.
Journal, issue, pagesNat Commun, Vol. 11, Page 5199-5199, Year 2020
Publish dateMar 8, 2018 (structure data deposition date)
AuthorsNowak, K. / Rosenthal, F. / Karlberg, T. / Butepage, M. / Thorsell, A.G. / Dreier, B. / Grossmann, J. / Sobek, J. / Imhof, R. / Luscher, B. ...Nowak, K. / Rosenthal, F. / Karlberg, T. / Butepage, M. / Thorsell, A.G. / Dreier, B. / Grossmann, J. / Sobek, J. / Imhof, R. / Luscher, B. / Schuler, H. / Pluckthun, A. / Leslie Pedrioli, D.M. / Hottiger, M.O.
External linksNat Commun / PubMed:33060572
MethodsX-ray diffraction
Resolution1.82 Å
Structure data

PDB-6fx7:
Crystal structure of in vitro evolved Af1521
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

Chemicals

ChemComp-AR6:
[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL

ChemComp-HOH:
WATER

Source
  • archaeoglobus fulgidus dsm 4304 (archaea)
KeywordsSIGNALING PROTEIN / Macro domain / ADP-ribose binding

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