User:Michael Skovbo Windahl/sandbox
From Proteopedia
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The <scene name='User:Michael_Skovbo_Windahl/sandbox/3e2t_iron_coordination/1'>iron is coordinated</scene> by 2 histidines, one glutamate and one imidazole from the solvent. | The <scene name='User:Michael_Skovbo_Windahl/sandbox/3e2t_iron_coordination/1'>iron is coordinated</scene> by 2 histidines, one glutamate and one imidazole from the solvent. | ||
| - | This coordination is called the 2-histidine-1-glutamate facial triad iron coordination and is seen in many mononuclear non-heme iron(II)enzymes<ref>PMID: 15739104</ref>. In this structure | + | This coordination is called the 2-histidine-1-glutamate facial triad iron coordination and is seen in many mononuclear non-heme iron(II)enzymes<ref>PMID: 15739104</ref>. In this structure Glu317 coordinates the iron in a partial bidentate manner. |
| + | <scene name='User:Michael_Skovbo_Windahl/sandbox/3e2t_trp_binding/1'>Tryptophan</scene> is bound in the active site. It is bound by polar contacts in the amino acid end and by hydrophobic interactons in the side chain end. | ||
==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 13:53, 7 April 2009
This is a sandbox
Tryptophan hydroxylase is an iron and tetrahydrobiopterin dependent monooxygenase which belongs to the enzyme family of aromatic amino acid hydroxylases.
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| 3e2t, resolution 1.90Å () | |||||||||
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| Ligands: | , , , , | ||||||||
| Activity: | Tryptophan 5-monooxygenase, with EC number 1.14.16.4 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
The by 2 histidines, one glutamate and one imidazole from the solvent. This coordination is called the 2-histidine-1-glutamate facial triad iron coordination and is seen in many mononuclear non-heme iron(II)enzymes[1]. In this structure Glu317 coordinates the iron in a partial bidentate manner.
is bound in the active site. It is bound by polar contacts in the amino acid end and by hydrophobic interactons in the side chain end.
References
- ↑ 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
