Sandbox Reserved 1758: Difference between revisions
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The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine. | The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine. | ||
== Structural highlights == | == Structural highlights == | ||
This enzyme is a <scene name='93/934002/Homodimer/1'>homodimer</scene>, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The | This enzyme is a <scene name='93/934002/Homodimer/1'>homodimer</scene>, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The <scene name='93/934002/Space-filling_view/1'>space-filling view</scene> of the protein shows the ligand covered by the enzyme with the polar end sticking out of the cavity. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
