Sandbox Reserved 1760: Difference between revisions

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== Important amino acids==

Amino Acids in the <scene name='93/934004/Plp_binding_site/6'>PLP binding site</scene> are Lys 292, Asp 263, Arg 180. They are essential to the active site by providing certain <scene name='93/934004/Plp_ligand/2'>interactions with PLP</scene>. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate group interacts with the positively charged nitrogen of the arginine side chain.

Amino Acids in the <scene name='93/934004/Plp_binding_site/6'>PLP binding site</scene> are Lys 292, Asp 263, Arg 180. They are essential to the active site by providing certain <scene name='93/934004/Plp_ligand/2'>interactions with PLP</scene>. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. Another interaction provided in this active site but not apart of the catalytic triad is the amino acid phenylalanine 177, there is a pi stacking interaction between its ring and the ring of the PLP.

== Structural highlights ==

The <scene name='93/934004/Binding_pocket/2'>binding pocket</scene> for PLP are semi-exposed to the "outside world" but also slightly hidden into the protein. Having binding pockets only slightly exposed can help prevent other competitive substrates from binding and and inhibiting the enzyme.

Sandbox Reserved 1760: Difference between revisions

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@@ Line 10: / Line 10: @@
 == Important amino acids==
-Amino Acids in the <scene name='93/934004/Plp_binding_site/6'>PLP binding site</scene> are Lys 292, Asp 263, Arg 180. They are essential to the active site by providing certain <scene name='93/934004/Plp_ligand/2'>interactions with PLP</scene>. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate group interacts with the positively charged nitrogen of the arginine side chain.
+Amino Acids in the <scene name='93/934004/Plp_binding_site/6'>PLP binding site</scene> are Lys 292, Asp 263, Arg 180. They are essential to the active site by providing certain <scene name='93/934004/Plp_ligand/2'>interactions with PLP</scene>. PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate group interacts with the positively charged nitrogen of the arginine side chain. Another interaction provided in this active site but not apart of the catalytic triad is the amino acid phenylalanine 177, there is a pi stacking interaction between its ring and the ring of the PLP.
 == Structural highlights ==
 The <scene name='93/934004/Binding_pocket/2'>binding pocket</scene> for PLP are semi-exposed to the "outside world" but also slightly hidden into the protein. Having binding pockets only slightly exposed can help prevent other competitive substrates from binding and and inhibiting the enzyme.