Kinases are one of the most studied protein families in medicinal chemistry, resulting in an amount of available data too large to be handled by a human brain. By combining a precise cartography of the ATP binding site and a tailored fragmentation method, KinFragLib allows to read, fragment, and organize by subpocket inhibitors co-crystallized with a kinase in the DFG-in conformation. The subsequent analysis of the chemical matter of the compiled fragments is in agreement with the general knowledge of medicinal chemists, identifying small and lipophilic fragments in the gatekeeper area, solubilizing fragments in the front pocket, and typical hinge binders for the adenine pocket. While this analysis is also in line with previous works conducted for the hinge binding fragments, this study provides for the first time a fragment library that is organized by subpocket, unveiling subpocket occupation and connection frequencies. It was found that chemically diverse fragments can bind the same subpocket. Furthermore, 79% of the identified fragments were only observed in one kinase structure, but the other 21% could bind the same subpocket of different kinase groups.