3e2t: Difference between revisions
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[[Image:3e2t_Trp_interactions.png| 500px]] | [[Image:3e2t_Trp_interactions.png| 500px]] | ||
The substrate specificity of TPH1 has been studied previously. These studies have shown that the substrate specificity i mainly controlled by Tyr236 and Phe314. Tyr236 is also involved in the binding of the tetrahydrobiopterin as seen in the structure of human TPH1 ([[1mlw]]). | |||
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Crystal structures of [[phenylalanine hydroxylase]] have been solved with a substrate analogue <scene name='User:Michael_Skovbo_Windahl/sandbox/1mmk_thienylalanine/1'>3-(2-thienyl)-alanine</scene> and tetrahydrobiopterin (entry [[1mmk]]). This structure shows the same compactness as the chicken TPH1 structure with an root mean square deviation of 0.94 Å. In comparison the chicken TPH1 and human TPH1 structure has an r.m.s.d. of 1.47 Å. | Crystal structures of [[phenylalanine hydroxylase]] have been solved with a substrate analogue <scene name='User:Michael_Skovbo_Windahl/sandbox/1mmk_thienylalanine/1'>3-(2-thienyl)-alanine</scene> and tetrahydrobiopterin (entry [[1mmk]]). This structure shows the same compactness as the chicken TPH1 structure with an root mean square deviation of 0.94 Å. In comparison the chicken TPH1 and human TPH1 structure has an r.m.s.d. of 1.47 Å. | ||
== Iron coordination == | == Iron coordination == | ||
