Sandbox GGC1
From Proteopedia
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== Chymotrypsin == | == Chymotrypsin == | ||
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'> | <StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'> | ||
| - | Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13, 16-146, 149-245) | + | Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. 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). |
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. | 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. | This is a default text for your page '''Chymotrypsin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
Revision as of 16:00, 10 April 2017
Chymotrypsin
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References
- ↑ Czapinska H, Helland R, Smalas AO, Otlewski J. Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants. J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809 doi:10.1016/j.jmb.2004.09.088
- ↑ Czapinska H, Helland R, Smalas AO, Otlewski J. Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants. J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809 doi:10.1016/j.jmb.2004.09.088
