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 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. | 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. | ||
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. | ||
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== References == | == References == | ||
<references/> | <references/> | ||