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. Author manuscript; available in PMC: 2019 Apr 16.
Published in final edited form as: Bioconjug Chem. 2018 Aug 31;29(9):3180–3195. doi: 10.1021/acs.bioconjchem.8b00514

Figure 3.

Figure 3.

Active site modeling of caspase-3 with substrates. (a) Active site of caspase-3 with pharmacophore docked pose of 16 in the closed configuration. Green represents hydrophobic and magenta hydrophilic surfaces. (b) Flexibility of the caspase-3 S2 pocket observed in crystal structures compared to the modeled closed conformation (green residues). (c) Binding of compound 16 in a flexible model of the caspase-3 active site. (d) Sequence alignment of the residues that define the S2 pocket of human caspases.