Figure 4 - full size


Figure 4.
Figure 4. The putative active site. The phosphate group of DHAP is half-encircled by the side-chain of Arg269, and interacts with Arg269 and Gly268 directly by hydrogen bonds (not shown). The conserved residues Lys204, Asn205, Asp260 and Thr264 form a stable hydrogen bonding network. The other hydrogen bonding network includes residues Lys120 and Asp260, as well as an ordered water molecule (with a B-factor of 16.4 Å2) which hydrogen bonds to Gly149 and Asn151 (not shown). In these two electrostatic networks, only the e-NH3+ group of Lys204 is the nearest to the C[2] atom of DHAP (3.4 Å).

The above figure is reprinted by permission from Elsevier: J Mol Biol (2006, 357, 858-869) copyright 2006.