Sandbox Reserved 1734: Difference between revisions
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Tertiary Structure: | Tertiary Structure: | ||
The tertiary structure of each monomer of PAH 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. 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). The catalytic domain includes the binding sites for iron, substrate and cofactor.The binding sites are at residues 285, 290, and 330. | The tertiary structure of each monomer of PAH 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. 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). The catalytic domain includes the binding sites for iron, substrate and cofactor.The binding sites are at residues 285, 290, and 330. The ACT domain is in the N-terminal regulatory domain where proposed enzyme binding to an allosteric site (residues 3-11). | ||
Quaternary Structure: | Quaternary Structure: | ||
