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TitleSulfoximine-substituted trifluoromethylpyrimidine analogs as inhibitors of proline-rich tyrosine kinase 2 (PYK2) show reduced hERG activity.
Journal, issue, pagesBioorg. Med. Chem. Lett., Vol. 19, Page 3253-3258, Year 2009
Publish dateApr 16, 2009 (structure data deposition date)
AuthorsWalker, D.P. / Zawistoski, M.P. / McGlynn, M.A. / Li, J.C. / Kung, D.W. / Bonnette, P.C. / Baumann, A. / Buckbinder, L. / Houser, J.A. / Boer, J. ...Walker, D.P. / Zawistoski, M.P. / McGlynn, M.A. / Li, J.C. / Kung, D.W. / Bonnette, P.C. / Baumann, A. / Buckbinder, L. / Houser, J.A. / Boer, J. / Mistry, A. / Han, S. / Xing, L. / Guzman-Perez, A.
External linksBioorg. Med. Chem. Lett. / PubMed:19428251
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-3h3c:
Crystal structure of PYK2 in complex with Sulfoximine-substituted trifluoromethylpyrimidine analog
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-P1E:
4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / PYK2 / Kinase / Alternative splicing / ATP-binding / Cell membrane / Cytoplasm / Membrane / Nucleotide-binding / Phosphoprotein / Polymorphism / Tyrosine-protein kinase

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