Sandbox Reserved 1056: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
To the left is the <scene name='75/752345/Hydrophobic_binding_pocket/1'>hydrophobic binding pocket</scene> of Carboxypeptidase A in ''B. Taurus,'' one of the molecules most important structural features. This binding pocket is the site at which C-terminal side chain of the substrate binds. It is formed by amino acid residues I243, I247, A250, G252, G253, S254 and I255. | |||
<Structure load='1CPX' size='350' frame='true' align='right' caption='This is a 3D image of Carboxypeptidase A in ''B. Taurus.'' ' scene='' /> | <Structure load='1CPX' size='350' frame='true' align='right' caption='This is a 3D image of Carboxypeptidase A in ''B. Taurus.'' ' scene='' /> | ||
Nearby, there is also Y198 which serves as the recognition site for the sidechain next to the C-terminal residue. | |||
== Mechanism of Action == | == Mechanism of Action == | ||
Revision as of 16:07, 14 March 2017
| This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080. |
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Carboxypeptidase A in B. taurusCarboxypeptidase A in B. taurus
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. IntroductionInstructionsClick above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [3] or to the article describing Jmol [4] to the rescue. Biological FunctionStructural Overview Structural highlightsTo the left is the of Carboxypeptidase A in B. Taurus, one of the molecules most important structural features. This binding pocket is the site at which C-terminal side chain of the substrate binds. It is formed by amino acid residues I243, I247, A250, G252, G253, S254 and I255.
Nearby, there is also Y198 which serves as the recognition site for the sidechain next to the C-terminal residue. Mechanism of ActionZinc Ligand(s)Other LigandsThis is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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ReferencesReferences
- ↑ 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
- ↑ 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
Bukrinsky, J.T., Bjerrum, M.J. and Kadziola, A. (1998), Native Carboxypeptidase A in a New Crystal Environment Reveals a Different Conformation of the Important Tyrosine 248. Biochem., 37:16555-16564.