Sandbox 156: Difference between revisions

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===The Acetyl-CoA Binding Site===

The binding of chloramphenicol blocks acetyl-CoA from entering the active site from the <scene name='Sandbox_156/~~Scene_8~~/1'>top of the enzyme</scene>, as illustrated. Instead, the second substrate tunnels to the active site through the <scene name='Sandbox_156/~~Scene~~/1'>pantetheine arm</scene> from the opposite side of the trimer. The amino acids lining the tunnel are also primarily lined with hydrophobic residues allowing for close contact between the substrate and aromatic residues<ref>PMID: 1544895</ref>. This tunneling allows the formation of van der Waals interactions between the adenine ring of acetyl-CoA with dimethyl groups of the pantetheine arm and hydrogen bonding of the ring with Tyr-56,Phe-96 and Phe-103, binding the substrate.

The binding of chloramphenicol blocks acetyl-CoA from entering the active site from the <scene name='Sandbox_156/Scene9/1'>top of the enzyme</scene>, as illustrated. Instead, the second substrate tunnels to the active site through the

<scene name='Sandbox_156/Scene9/2'>pantetheine arm</scene> from the opposite side of the trimer. The amino acids lining the tunnel are also primarily lined with hydrophobic residues allowing for close contact between the substrate and aromatic residues<ref>PMID: 1544895</ref>. This tunneling allows the formation of van der Waals interactions between the adenine ring of acetyl-CoA with dimethyl groups of the pantetheine arm and hydrogen bonding of the ring with Tyr-56,Phe-96 and Phe-103, binding the substrate.

===The Active Site===

Sandbox 156: Difference between revisions

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@@ Line 30: / Line 30: @@
 ===The Acetyl-CoA Binding Site===
-The binding of chloramphenicol blocks acetyl-CoA from entering the active site from the <scene name='Sandbox_156/Scene_8/1'>top of the enzyme</scene>, as illustrated. Instead, the second substrate tunnels to the active site through the <scene name='Sandbox_156/Scene/1'>pantetheine arm</scene> from the opposite side of the trimer. The amino acids lining the tunnel are also primarily lined with hydrophobic residues allowing for close contact between the substrate and aromatic residues<ref>PMID: 1544895</ref>. This tunneling allows the formation of van der Waals interactions between the adenine ring of acetyl-CoA with dimethyl groups of the pantetheine arm and hydrogen bonding of the ring with Tyr-56,Phe-96 and Phe-103, binding the substrate.
+The binding of chloramphenicol blocks acetyl-CoA from entering the active site from the <scene name='Sandbox_156/Scene9/1'>top of the enzyme</scene>, as illustrated. Instead, the second substrate tunnels to the active site through the
+<scene name='Sandbox_156/Scene9/2'>pantetheine arm</scene> from the opposite side of the trimer. The amino acids lining the tunnel are also primarily lined with hydrophobic residues allowing for close contact between the substrate and aromatic residues<ref>PMID: 1544895</ref>. This tunneling allows the formation of van der Waals interactions between the adenine ring of acetyl-CoA with dimethyl groups of the pantetheine arm and hydrogen bonding of the ring with Tyr-56,Phe-96 and Phe-103, binding the substrate.
 ===The Active Site===