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. Author manuscript; available in PMC: 2019 Aug 20.
Published in final edited form as: ChemMedChem. 2018 Jul 11;13(16):1681–1694. doi: 10.1002/cmdc.201800188

Figure 2. Structure of WEE1 inhibitors AZD1775 and CM-061 (1) and predicted WEE1-AZD1775 interactions.

Figure 2.

(A) Ribbon representation (blue ribbon, grey amino acid residues; with clipped pane molecular surface colored dark grey) of the ATP-binding site of WEE1 displaying the predicted binding mode of AZD1775 (cyan). Red dashed lines indicate H-bonds and yellow dashed lines indicate π-π interactions. (B) A stick display style representation of AZD1775 (cyan) and key interacting amino acid residues and target residues (grey) for inhibitor design. Red dashed lines indicate H-bonds and yellow dashed lines indicate π-π interactions. (C) Ligand interaction diagram of the predicted binding mode of AZD1775 in the ATP-binding site of WEE1. Red residues are charged negative, purple residues are charged positive, green residues are hydrophobic, and blue residues are polar, purple arrows indicate H-bonds, green lines indicate π-π interactions, and grey circles indicate areas of solvent exposure. (D) The chemical structure of the WEE1 inhibitors AZD1775 and CM-061 (1).