Sandbox Reserved 1763: Difference between revisions

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Amino Acids in PLP binding site are Lys 292, Asp 263, and Arg 180. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.

== Structural highlights ==

hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The ligand has a phosphate group surrounded by polar amino acids, carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.

hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Sandbox Reserved 1763: Difference between revisions

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@@ Line 15: / Line 15: @@
 Amino Acids in PLP  binding site are Lys 292, Asp 263, and Arg 180. They are essential to the active site. PLP is covalently bonded to the amino acid lysine. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. There is also a pi-stacking interaction between its ring and the ring of PLP.
 == Structural highlights ==
-hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The ligand has a phosphate group surrounded by polar amino acids, carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
+hOAT is a protein with a secondary structure consisting of mainly alpha-helices but it also has parallel and anti-parallel beta-sheets and random coil. It's a polymer with a globular structure that has three subunits held together by non-covalent interactions such as hydrogen bonds and salt bridges hidden in the protein. The <scene name='93/934007/Ligands_of_interest/1'>ligand</scene> has a phosphate group surrounded by polar amino acids, carbons are surrounded by non-polar amino acids to satisfy the needs of the ligand and active site. Interactions like hydrogen bonding and pi-stacking stabilize and bind the ligand in the active site.
 This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.