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 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). 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.