Tryptophan hydroxylase 1 with bound tryptophan

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PDB ID 3e2t

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About this Structure

3E2T is a 1 chain structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Additional Resources

For additional information, see: Amino Acid Synthesis & Metabolism


  • Windahl MS, Petersen CR, Christensen HE, Harris P. Crystal Structure of Tryptophan Hydroxylase with Bound Amino Acid Substrate. Biochemistry. 2008 Oct 21. PMID:18937498 doi:10.1021/bi8015263
  • Nielsen MS, Petersen CR, Munch A, Vendelboe TV, Boesen J, Harris P, Christensen HE. A simple two step procedure for purification of the catalytic domain of chicken tryptophan hydroxylase 1 in a form suitable for crystallization. Protein Expr Purif. 2008 Feb;57(2):116-26. Epub 2007 Nov 20. PMID:18055219 doi:10.1016/j.pep.2007.10.016
  1. Jiang GC, Yohrling GJ 4th, Schmitt JD, Vrana KE. Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling. J Mol Biol. 2000 Sep 29;302(4):1005-17. PMID:10993738 doi:10.1006/jmbi.2000.4097
  2. McKinney J, Teigen K, Froystein NA, Salaun C, Knappskog PM, Haavik J, Martinez A. Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity. Biochemistry. 2001 Dec 25;40(51):15591-601. PMID:11747434
  3. Daubner SC, Moran GR, Fitzpatrick PF. Role of tryptophan hydroxylase phe313 in determining substrate specificity. Biochem Biophys Res Commun. 2002 Apr 5;292(3):639-41. PMID:11922614 doi:10.1006/bbrc.2002.6719
  4. Koehntop KD, Emerson JP, Que L Jr. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J Biol Inorg Chem. 2005 Mar;10(2):87-93. Epub 2005 Mar 1. PMID:15739104 doi:10.1007/s00775-005-0624-x

Created with the participation of Michael Skovbo Windahl, Eran Hodis, David Canner.

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Alexander Berchansky

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