Sandbox Reserved 1734: Difference between revisions

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Tertiary Structure:

The tertiary structure of each monomer of phenylalanine hydroxylase is organized from 2 alpha helices and 4 beta-strands into an alpha-beta sandwich motif (BaBBaB fold). The structural motif of an alpha-beta sandwich motif has the 4 antiparallel beta-strands flanked on one side by the 2 alpha-helices (3 & 5). The tertiary structure of a phenylalanine hydroxylase protein is built from an N-terminal regulatory domain (residues 1-117), a catalytic domain (residues 118-410), and a tetramerization domain (residues 411-452) (3 & 6). The catalytic domain includes the binding sites for iron, substrate, and cofactor. The binding sites are at residues 285, 290, and 330. The archetypical (ACT) domain is in the N-terminal regulatory domain where the proposed enzyme binding to an allosteric site (residues 3-11) (6).

The <scene name='91/919043/Tertiary_struc_of_monomer/1'>tertiary structure</scene> of each monomer of phenylalanine hydroxylase is organized from 2 alpha helices and 4 beta-strands into an alpha-beta sandwich motif (BaBBaB fold). The structural motif of an alpha-beta sandwich motif has the 4 antiparallel beta-strands flanked on one side by the 2 alpha-helices (3 & 5). The tertiary structure of a phenylalanine hydroxylase protein is built from an N-terminal regulatory domain (residues 1-117), a catalytic domain (residues 118-410), and a tetramerization domain (residues 411-452) (3 & 6). The catalytic domain includes the binding sites for iron, substrate, and cofactor. The binding sites are at residues 285, 290, and 330. The archetypical (ACT) domain is in the N-terminal regulatory domain where the proposed enzyme binding to an allosteric site (residues 3-11) (6).

Quaternary Structure:

Sandbox Reserved 1734: Difference between revisions

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@@ Line 12: / Line 12: @@
 Tertiary Structure:
-The tertiary structure of each monomer of phenylalanine hydroxylase is organized from 2 alpha helices and 4 beta-strands into an alpha-beta sandwich motif (BaBBaB fold). The structural motif of an alpha-beta sandwich motif has the 4 antiparallel beta-strands flanked on one side by the 2 alpha-helices (3 & 5). The tertiary structure of a phenylalanine hydroxylase protein is built from an N-terminal regulatory domain (residues 1-117), a catalytic domain (residues 118-410), and a tetramerization domain (residues 411-452) (3 & 6). The catalytic domain includes the binding sites for iron, substrate, and cofactor. The binding sites are at residues 285, 290, and 330. The archetypical (ACT) domain is in the N-terminal regulatory domain where the proposed enzyme binding to an allosteric site (residues 3-11) (6).
+The <scene name='91/919043/Tertiary_struc_of_monomer/1'>tertiary structure</scene> of each monomer of phenylalanine hydroxylase is organized from 2 alpha helices and 4 beta-strands into an alpha-beta sandwich motif (BaBBaB fold). The structural motif of an alpha-beta sandwich motif has the 4 antiparallel beta-strands flanked on one side by the 2 alpha-helices (3 & 5). The tertiary structure of a phenylalanine hydroxylase protein is built from an N-terminal regulatory domain (residues 1-117), a catalytic domain (residues 118-410), and a tetramerization domain (residues 411-452) (3 & 6). The catalytic domain includes the binding sites for iron, substrate, and cofactor. The binding sites are at residues 285, 290, and 330. The archetypical (ACT) domain is in the N-terminal regulatory domain where the proposed enzyme binding to an allosteric site (residues 3-11) (6).
 Quaternary Structure: