Description

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.


Links:

• Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell 94: 161-170 (1998)


• PDB entry


• PDB summary


• SCOP structural classification

Instructions

• 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.



• You can download the pdf file here

• To display and manipulate the structure, you need at least Adobe Acrobat Reader v7.0. For best results, install the last version of Acrobat Reader.


• To hide/show elements in the structure, first you have to click inside the render window.