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). 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 or to the article describing Jmol to the rescue. Function The active site of chymotrypsin consists of a catalytic triad (Ser 195, His 57, Asp 102), which are highlighted in blue. The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The S1 pocket of the bovine alpha-chymotrypsin is highlighted in yellow. Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids, and the S1 binding pocket helps stabilize the intermediate before completely cleaving the amino acid. Both the active site and S1 pocket can be seen here. The catalytic triad is highlighted in blue and the S1 pocket is highlighted 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.