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TitleOptimization of pyrazolo[1,5-a]pyrimidines lead to the identification of a highly selective casein kinase 2 inhibitor.
Journal, issue, pagesEur. J. Med. Chem., Vol. 208, Page 112770-112770, Year 2020
Publish dateApr 27, 2020 (structure data deposition date)
AuthorsKramer, A. / Kurz, C.G. / Berger, B.T. / Celik, I.E. / Tjaden, A. / Greco, F.A. / Knapp, S. / Hanke, T.
External linksEur. J. Med. Chem. / PubMed:32883634
MethodsX-ray diffraction
Resolution2.4 - 2.75 Å
Structure data

PDB-6yul:
CK2 alpha bound to Macrocycle
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6yum:
CK2 alpha bound to unclosed Macrocycle
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PQ5:
7,10-Dioxa-13,17,18,21-tetrazatetracyclo[12.5.2.12,6.017,20]docosa-1(20),2(22),3,5,14(21),15,18-heptaene-5-carboxylic acid

ChemComp-HOH:
WATER

ChemComp-PQ8:
4-[5-[2-(2-hydroxyethyloxy)ethyl-[(2-methylpropan-2-yl)oxycarbonyl]amino]pyrazolo[1,5-a]pyrimidin-3-yl]-2-oxidanyl-benzoic acid

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Kinase / Macrocycle / Inhibitor / Structural Genomics / Structural Genomics Consortium / SGC

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