A Novel Inhibitor of Mammalian Triosephosphate Isomerase Found by an In Silico Approach

Figure 5

TIM binding site hydrophobicity map. The regions that a ligand encounters during binding to TIM are shown in a course-feature heatmap to emphasize broad regions of hydrophobicity and hydrophilicity in the site. Two significant hydrophobic regions and two hydrophilic regions are shown. Blue, hydrophobic; light blue, partially hydrophobic. Green, hydrophilic; light green, partially hydrophilic. The binding site was centered on binding of the substrate analog 2-phosphoglycolic acid. Flanking residues were extended manually based on topological association with the binding pocket. The lower hydrophobic region represents the active site loop region. The central hydrophilic region includes the catalytic domain and part of the phosphate-binding region. The upper hydrophobic region includes weakly hydrophobic residues that make up the bulk of the phosphate binding site and more strongly hydrophobic residues that make up the extended pocket.