Molecular docking of substituted pteridinones and pyrimidines to the ATP-binding site of the N-terminal domain of RSK2 and associated MM/GBSA and molecular field datasets

. 2020 Feb 28;29:105347. doi: 10.1016/j.dib.2020.105347

Value of the Data

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The RSK2 kinase has been identified as a molecular target for the treatment of various cancer types.
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The pteridinones and pyrimidines comprised a structure-activity study for BI-D1870, a potent pan-RSK inhibitor.
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The modeling data was generated to guide the structure-activity study and to rationalize the structural requirements for RSK inhibition.
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The binding confirmations of the pteridinones and pyrimidines, their interactions with RSK2 and calculated binding energies may inform further studies focused on the development of RSK inhibitors.
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The molecular field models for the RSK inhibitors in their docked conformations provides additional information in terms of favourable electronics for RSK inhibitor binding.