Sandbox GGC1

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== Chymotrypsin ==
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==Chymotrypsin== 0
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<StructureSection load='1T8L' size='340' side='right' caption='Bovine α-Chymotrypsin' scene='75/752263/Intro/1'>
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref>
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This is a default text for your page '''Sandbox GGC1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Structural Highlights and Function ==
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== Function ==
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Chymotrypsinogen is the inactive form of chymotrypsin. Before chymotrypsinogen becomes α-chymotrypsin, trypsin cleaves the polypeptides at three locations: between residues 14-15, 146-147, and 148-149. The resulting α-chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow.
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The S1 binding pocket is responsible for stabilizing the substrate before the enzyme cleaves the peptide bond. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes Phe, Tyr, and Trp. 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.
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== Disease ==
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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 a monomer is highlighted <scene name='75/752263/S1_pocket_active_site/1'>here</scene>.
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== Relevance ==
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== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/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.
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 23:34, 19 February 2018

==Chymotrypsin== 0

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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