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.