Receptor-interacting serine/threonine protein kinase 1 (RIPK1) has emerged as a compelling therapeutic target for inflammatory and neurodegenerative diseases. Most advanced RIPK1 inhibitors act through a type III mechanism, occupying an allosteric pocket adjacent to the ATP site and stabilizing the inactive, DLG-out conformation. While this establishes the allosteric pocket as a tractable site, the inhibitors reported to date are drawn from a limited range of scaffolds. We therefore undertook a virtual screening campaign directed at scaffolds structurally distinct from the known chemotypes. Pharmacophore hypotheses were derived from 8 reported type III inhibitor PDB structures and ranked by enrichment factor, and the top-performing hypothesis was applied to the Korea Chemical Bank library. Retrieved compounds were successively filtered by molecular docking, MM-GBSA binding energy calculation, and MD simulation. The screen recovered scaffolds of known type III inhibitors, confirming that the hypothesis captures the pharmacophoric features of authentic allosteric binders. Among the 53 candidates evaluated in the ADP-Glo kinase assay, one compound distinct from the reference inhibitors inhibited RIPK1 by 65.5% at 10 µM, corroborating the in silico predictions. By coupling virtual screening with experimental validation, this work extends the scaffold repertoire available at the RIPK1 allosteric site and provides future work on structure-based optimization of the identified hit.