A number of fragments (3, 6, 10, 25, 34, 35, 36, 42, and 47) were found to bind into a pocket formed in the dimer interface close to the fatty acid binding site (Figure and). This pocket, like the fatty acid binding site, is formed primarily by hydrophobic residues. Furthermore, this pocket is symmetric as the residues that form the pocket are the same in both chains. Accordingly, the hit compounds that bind into this pocket could be modelled in two orientations (Figure and Figure ). These compounds form hydrogen bonds with backbone protein atoms as well as water molecules, which act as hydrogen-bond bridges between the ligands and the protein. When superimposing the structures with these fragments bound, it becomes evident that these fragments overlap and combined fill the entire pocket (Figure ).