We have conducted a fragment screen using X-ray crystallography for PaFabF using the covalent intermediate state mimicking variant C164Q. Five points stand out from this study: 1) Many different binding sites for fragments where identified, but only few fragments bound into or close to the substrate binding sites. 2) No binding affinity for the hit fragments of interest could be measured using BLI. The same was observed for fragments mimicking the benzoic acid moiety of the potent natural product ligands platencin and platensimycin. 3) Synthesis of analogues of one the hits resulted in ligands with affinities in the micromolar range. 4) The data package forms a strong foundation for the development of more potent FabF inhibitors. We expand on these points below.