Sandbox Reserved 1056: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
[[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.]]
[[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.]]
To the left is the <scene name='69/694223/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.
Shown to the left is the hydrophobic binding pocket of Carboxypeptidase A in ''B. taurus'' in relation to the whole molecule. It is one of the molecule's most important structural features. The <scene name='69/694223/Hydrophobic_binding_pocket_2/2'>hydrophobic binding pocket</scene> is also isolated in the 3D applet to the right. 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.
Nearby, there is also Y198 which serves as the recognition site for the sidechain next to the C-terminal residue.

Latest revision as of 16:49, 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

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.

Introduction

Biological Function

Structural Overview

Structural highlights

Carboxypeptidase A in B. taurus. The red highlights the hydrophobic binding pocket while the blue highlights Y248.

Shown to the left is the hydrophobic binding pocket of Carboxypeptidase A in B. taurus in relation to the whole molecule. It is one of the molecule's most important structural features. The is also isolated in the 3D applet to the right. 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 Action

Zinc Ligand(s)

Other Ligands

This 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.


Caption for this structure

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ReferencesReferences

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Braden Sciarra, Garrett Oberst, Geoffrey C. Hoops, Douglas Schnell
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