Sandbox GGC1

Chymotrypsin

spinqualitylabelsall models Bovine chymotrypsin complexes with P1 BPTI variants Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of three chains (residues 1-13, 16-146, 149-245) The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage. This is a default text for your page Chymotrypsin. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Chymotrypsin Function Active Site is in yellow Structural highlights This is a sample scene created with SAT to color by Group, and another to make Text To Be Displayed456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.