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. Author manuscript; available in PMC: 2016 Dec 15.
Published in final edited form as: Nature. 2016 Jun 15;534(7608):570–574. doi: 10.1038/nature18002

Figure 2. Analysis of cysteines and proteins liganded by fragment electrophiles.

Figure 2

a, Fraction of total quantified cysteines and proteins that were liganded by fragment electrophiles in competitive isoTOP-ABPP experiments. b, Fraction of liganded proteins found in DrugBank. c, Functional classes of DrugBank and non-DrugBank proteins containing liganded cysteines. d, Comparison of the ligandability of cysteines as a function of their intrinsic reactivity with the IA-alkyne probe. Cysteine reactivity values (left y-axis) were taken from reference12, where lower ratios correspond to higher cysteine reactivity. A moving average with a step-size of 50 is shown in blue for the percentage of liganded cysteines within each reactivity bin (percent values shown on right y-axis).