Structure of a angiotensin-converting enzyme in complex with lisinopril. The overall fold of this metalloprotease is similar to that of neurolysin. The catalytic domain consists of two alpha helix rich subdomains. A deep cleft between those subdomains harbors the catalytic site. The catalytic site of this protease contains a Zn atom (shown as a golden sphere) complexed by His414, His418, and Asp442. It also contains Glu415, which is supposed to provide a general base to attack the target peptidic bond by interacting with a water molecule.
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.