Figure 4.

The hydrophobic substrate-binding pocket of PRCP. The putative proline-binding pocket is formed by Trp 432 and Trp 359 based on structural identity with other prolyl peptidases and the spatial alignment with the Ser 179-His 455-Asp 430 catalytic triad.

Soisson et al. BMC Structural Biology 2010 10:16   doi:10.1186/1472-6807-10-16
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