Typically, FBDD starts with the screening of a fragment library to identify binders to specific targets, and only these hits are optimized into larger compounds by fragment linking or fragment growing. The screening step can be done experimentally or in silico. In the context of kinase inhibition, Urich et al. extracted ∼6,000 fragments with hinge-binding motifs from a kinase-unfocused library of 2.3 million compounds and docked them against 46 kinase structures to identify potential hinge binders. Fragment expansion of promising hits yielded a number of potent kinase inhibitors. Rachman et al. reported a potent hinge binding fragment, selected from a kinase-unfocused fragment library (624 fragments) via docking against the JAK2 ATP binding site, filtered by (i) pharmacophoric restraints (re-strained docking) at the hinge region and (ii) interaction strength measured by the work necessary to break a defined hinge hydrogen bond (dynamic undocking). However, it is also possible to start off directly with a kinase-focused library of fragments that provide optimal interaction patterns with the ATP binding site. For instance, Mukherjee et al. report the Kinase Crystal Miner to extract the smallest possible fragment in each kinase-ligand crystal structure with hydrogen bonds to the hinge region, yielding about 1,000 fragments from 2,250 ligands. Substructure searches for these fragments in large molecule databases supplied molecules with kinase binding potential. Note that all the aforementioned approaches make use of 3D structural information and focus on hinge-binding fragments to be used for fragment expansion or substructure searches in compound libraries.