Sandbox Reserved 1091
From Proteopedia
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== Function == | == Function == | ||
| - | + | The ASP protein is a serine protease of the subtilisin family. | |
== Structure == | == Structure == | ||
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| + | The ASP protein contains an N-terminal region that forms the subtilisin domain and a C-terminal region that forms the P-domain. | ||
| + | The subtilisin domain is composed of ten helices and twelve chains. The structure of the P-domain is a jelly roll-like fold with eight beta-strands. | ||
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| + | The structure contains calcium ions. | ||
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| + | The catalytic triad of ASP is composed of Asp78, His115 and Ser336. | ||
== Disease == | == Disease == | ||
Revision as of 22:16, 27 December 2019
| This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115. |
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References
- ↑ 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
- ↑ 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
