Sandbox GGC1: Difference between revisions
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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 <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow. | 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 <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow. | ||
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. | Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. | ||
<scene name='75/752263/S1_pocket_active_site/1'> | |||
The serine, histidine, and aspartate residues from the catalytic triad forms hydrogen bonds between each other. The structure of the binding and active site of one chain is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
