User:Michael Skovbo Windahl/sandbox
From Proteopedia
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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. | 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. | + | <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. <scene name='User:Michael_Skovbo_Windahl/sandbox/3e2t_tryptophan_pocket/1'>Trp binding residues</scene> |
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| + | <scene name='User:Michael_Skovbo_Windahl/sandbox/3e2t_tryptophan_pocket/2'>TextToBeDisplayed</scene> | ||
The <scene name='User:Michael_Skovbo_Windahl/sandbox/3e2t_imidazole_bind/2'>imidazole</scene> is bound to the iron and to the protein chain through two brigding water molecules. This binding is similar to the dihydrobiopterin binding in structure of the catalytic domain of human TPH1 [1mlw]. See the dihydrobiopterin binding <scene name='User:Michael_Skovbo_Windahl/sandbox/1mlw_iron_coordination/1'>iron coordination in 1mlw</scene> | The <scene name='User:Michael_Skovbo_Windahl/sandbox/3e2t_imidazole_bind/2'>imidazole</scene> is bound to the iron and to the protein chain through two brigding water molecules. This binding is similar to the dihydrobiopterin binding in structure of the catalytic domain of human TPH1 [1mlw]. See the dihydrobiopterin binding <scene name='User:Michael_Skovbo_Windahl/sandbox/1mlw_iron_coordination/1'>iron coordination in 1mlw</scene> | ||
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==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 09:48, 15 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.
The is bound to the iron and to the protein chain through two brigding water molecules. This binding is similar to the dihydrobiopterin binding in structure of the catalytic domain of human TPH1 [1mlw]. See the dihydrobiopterin binding
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
