Description

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.


Links:

• Crystal structure of the catalytic domain of human ADAM33. J Mol Biol 335: 129-137 (2004)


• 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.