Sandbox Reserved 1056: Difference between revisions

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

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