Sandbox Reserved 1844: Difference between revisions

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=== Ligand Binding Pocket ===

The <scene name='10/1075246/4eb0_with_colored_ligand_stick/3'>substrate-binding site</scene> of LCC is a long, mainly hydrophobic groove that accommodates PET chains. This groove includes three subsites—designated −2, −1, and +1—that interact with specific PET units near the scissile ester bond. Hydrophobic residues such as <scene name='10/1075248/4eb0_with_colored_ligand_stick/2'>F125, V212, M166, and F243</scene> line the groove and facilitate binding by interacting with the [https://en.wikipedia.org/wiki/Aromatic_compound aromatic] rings of the PET molecule. These interactions help align the substrate in the correct position for catalysis.

The <scene name='10/1075246/4eb0_with_colored_ligand_stick/5'>substrate-binding site</scene> of LCC is a long, mainly hydrophobic groove that accommodates PET chains. This groove includes three subsites—designated −2, −1, and +1—that interact with specific PET units near the scissile ester bond. Hydrophobic residues such as <scene name='10/1075248/4eb0_with_colored_ligand_stick/2'>F125, V212, M166, and F243</scene> line the groove and facilitate binding by interacting with the [https://en.wikipedia.org/wiki/Aromatic_compound aromatic] rings of the PET molecule. These interactions help align the substrate in the correct position for catalysis.

The <scene name='10/1075248/4eb0_surface_w_stick_ligand/1'>molecular surface view of the enzyme-ligand interaction</scene> shows the overall shape and depth of the binding groove. The <scene name='10/1075246/4eb0_hydrophobicity_ligand/3'>cartoon representation of the enzyme-ligand interaction</scene>, the enzyme is shown as a ribbon diagram with the hydrophobic residues colored pink, to show how the PET chain fits snugly into the groove.

Sandbox Reserved 1844: Difference between revisions

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 === Ligand Binding Pocket ===
-The <scene name='10/1075246/4eb0_with_colored_ligand_stick/3'>substrate-binding site</scene> of LCC is a long, mainly hydrophobic groove that accommodates PET chains. This groove includes three subsites—designated −2, −1, and +1—that interact with specific PET units near the scissile ester bond. Hydrophobic residues such as <scene name='10/1075248/4eb0_with_colored_ligand_stick/2'>F125, V212, M166, and F243</scene> line the groove and facilitate binding by interacting with the [https://en.wikipedia.org/wiki/Aromatic_compound aromatic] rings of the PET molecule. These interactions help align the substrate in the correct position for catalysis.
+The <scene name='10/1075246/4eb0_with_colored_ligand_stick/5'>substrate-binding site</scene> of LCC is a long, mainly hydrophobic groove that accommodates PET chains. This groove includes three subsites—designated −2, −1, and +1—that interact with specific PET units near the scissile ester bond. Hydrophobic residues such as <scene name='10/1075248/4eb0_with_colored_ligand_stick/2'>F125, V212, M166, and F243</scene> line the groove and facilitate binding by interacting with the [https://en.wikipedia.org/wiki/Aromatic_compound aromatic] rings of the PET molecule. These interactions help align the substrate in the correct position for catalysis.
 The <scene name='10/1075248/4eb0_surface_w_stick_ligand/1'>molecular surface view of the enzyme-ligand interaction</scene> shows the overall shape and depth of the binding groove. The <scene name='10/1075246/4eb0_hydrophobicity_ligand/3'>cartoon representation of the enzyme-ligand interaction</scene>, the enzyme is shown as a ribbon diagram with the hydrophobic residues colored pink, to show how the PET chain fits snugly into the groove.