Structure of human glutamate carboxypeptidase II. The fold of this catalytic domain is related to aminopeptidases from Aeromonas proteolytica.
The catalytic site of this protease contains two Zn atoms (shown as a golden spheres). Zinc 1 is complexed by Glu425 and His553, whereas zinc 2 is complexed by His337 and Asp387. On the other hand, Asp387 and a water molecule form "bridges" and complex both Zn atoms. According to its position, the putative general base which attacks the target peptidic bond depends on Glu424.



  • 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.