Structure of pig prolyl oligopeptidase in complex with z-pro-prolinal. This structure contains two domains. The N-terminal domain is proteolytic and, according to its overall fold, belongs to the SC clan. The C-terminal domain displays a beta propeller fold and is supposed to regulate proteolysis by the N-terminal domain. The catalytic site consists of a triad of residues in a charge relay system*, from Asp641 to His680 to Ser554. *See family S10 for a more detailed explanation of the charge relay system in a catalytic triad.
Structures are rendered as ribbons. Catalytic and catalytic metal-complexing residues are shown as neons. Inhibitors are displayed as space filling spheres.
Carbons are shown in light gray, hydrogens in cyan, oxygens in red, nitrogens in blue, and sulfurs in yellow.
Left-click and drag to rotate the protease. Right-click and drag up/down to zoom in/out. Click with both buttons and drag to move the protease. Use the upper bar to get different views and for display options. For a close-up of the catalytic site, choose the cat_site view.
Once you have clicked inside the structure window, you can use the keyboard to hide/show objects:
'1' toggles the ribbon. '2' toggles the inhibitor. '3' toggles the catalytic residues.