is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine alpha-chymotrypsin.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
The S1 binding pocket is responsible for stabilization of the substrate prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The of the bovine alpha-chymotrypsin is highlighted in yellow.
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make 456/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.
