Structure of human neprilysin. This metalloprotease shows a thermolysin-like fold. The catalytic site of this protease contains a Zn atom (shown as a golden sphere) complexed by His584, His588, and Glu647. It also contains Glu585, which is supposed to provide a general base to attack the target peptidic bond by interacting with a water molecule. See family M03 for an example of this interaction.
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.