Sandbox Reserved 1056

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== Structural Overview ==
== Structural Overview ==
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[[Image:Hydrophobic_C-terminal_Side_Chain_Binding_Site_with_Y248.png|100 px|left|thumb|Figure Legend]]
 
== Structural highlights ==
== Structural highlights ==
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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.
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[[Image:Hydrophobic_C-terminal_Side_Chain_Binding_Site_with_Y248.png|200 px|left|thumb|Carboxypeptidase A in ''B. taurus.'' The red highlights the hydrophobic binding pocket while the blue highlights Y248.]]
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<Structure load='1CPX' size='350' frame='true' align='right' caption='This is a 3D image of Carboxypeptidase A in ''B. Taurus.'' ' scene='' />
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To the left is the hydrophobic binding pocket 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.
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Nearby, there is also Y198 which serves as the recognition site for the sidechain next to the C-terminal residue.
Nearby, there is also Y198 which serves as the recognition site for the sidechain next to the C-terminal residue.

Revision as of 13:14, 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. taurus

Caption for this structure

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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
  3. ↑ 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
  4. ↑ 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.

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