Skip to main content
. 2013 Jul 25;9(7):e1003159. doi: 10.1371/journal.pcbi.1003159

Figure 1. Allosteric binding site of PYK with the activator FBP bound.

Figure 1

Residues V400 to V411, K446 to F470 and S481 to Q496 of the crystallographically resolved Saccharomyces cerevisiae PYK (PDB id: 1A3W, chain A) are shown in cartoon representation. Panel A shows possible hydrogen bonds between the FBP phosphate groups and the residues of PYK within a distance of 3 Å (all in stick representation). The structural P-loop motif (STSG) is coloured in purple. Panel B illustrates the phosphate interaction sites computed with the GRID program. The binding site of the 1′-phosphate moiety of FBP in the allosteric site is referred to as 1′Pibs and that of the 6′-phosphate moiety of FBP as 6′Pibs. The interaction energy is displayed at isocontours of −10 kcal/mol (mesh surface) and −13.5 kcal/mol (solid surface). Only the phosphate interaction sites that are located within 6 Å around FBP are shown.