Several preferred binding sites for fragments were identified and some fragments bound in more than one location (Figure and Table , Table ). Most fragments (28) were found to bind to 6 different crystal interfaces whereas 2 of these are related since PaFabF is a dimer. Further, 9 fragments bound into a dimer interface pocket next to the fatty acid binding site and another 8 fragments into a dimer interface pocket about 22 Å away from the catalytic histidines. Finally, 3 fragments bound adjacent to the entrance of the active site and 2 fragments each bound close to the catalytic residues of PaFabF and into the fatty acid binding site. In addition, 6 fragments bound at a position where no other fragment was found. None of these positions were close to the fatty acid binding site or the active site. We consider the fragments binding into the fatty acid binding site, the active site or close to these pockets to be of highest interest for drug discovery and a more detailed description of their binding modes follows below. Table . List with fragments binding in or close to the malonyl-CoA binding site, the fatty acid binding site, or the adjacent dimer interface pocket together with chemical structures of the ligands, binding site location, resolution of the crystal structures and PDB IDs. The PanDDA event maps for these ligands are displayed in Figure . molecules that act as hydrogen bond bridges between the ligand and surrounding protein residues. The distance between the nitrogen atom of the His304 ring and one of the oxygen atoms of the carboxylic group of hit 20 is 2.8 Å indicating that there is a hydrogen bond between these atoms. At the same time, the distance between the centres of the aromatic rings of hit 20 and His304 is 5.0 Å indicating favourable π-π interaction between the two residues. Compound 20 and the natural product ligands platencin and platensimycin (Figure ) share a 3-amino-benzoic acid motif. However, compound 20 bound nearly perpendicular compared to the benzene ring found in the natural products (Figure ). Nevertheless, the carboxylic acid groups of the ligands were found in the same position.