Sandbox Reserved 431
From Proteopedia
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[[Student Projects for UMass Chemistry 423 Spring 2016]] | [[Student Projects for UMass Chemistry 423 Spring 2016]] | ||
| + | <StructureSection load='1xcs' size='350' side='right' caption='caption for Molecular Playground (PDB entry [[1xcs]])' scene=''> | ||
==Introduction== | ==Introduction== | ||
| - | <Structure load='3c6g' size='300' frame='true' align='right' caption='pdbcode, Insert caption here' scene='Insert optional scene name here' /> | ||
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| - | <br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br> | ||
==Overall Structure== | ==Overall Structure== | ||
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- Asymmetric dimer <br> | - Asymmetric dimer <br> | ||
- Consists of α-helices, β-sheets (mostly on one side of the molecule) with a heme buried inside the protein <br> | - Consists of α-helices, β-sheets (mostly on one side of the molecule) with a heme buried inside the protein <br> | ||
- Two molecules of 2-hydroxypropyl-β-cyclodextrin are found near the dimer interface <br> | - Two molecules of 2-hydroxypropyl-β-cyclodextrin are found near the dimer interface <br> | ||
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==Binding Interactions== | ==Binding Interactions== | ||
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<scene name='48/483888/Secondary_structure/2'>Secondary Structure</scene> | <scene name='48/483888/Secondary_structure/2'>Secondary Structure</scene> | ||
-catalyzes initial step for converting vitamin D into 25-hydroxyvitamin D | -catalyzes initial step for converting vitamin D into 25-hydroxyvitamin D | ||
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-has closed conformation, substrate access channel mostly covered | -has closed conformation, substrate access channel mostly covered | ||
-secosteroid binding, extended active site | -secosteroid binding, extended active site | ||
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==Additional Features== | ==Additional Features== | ||
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This molecule has a heme which is bound to iron, which, combined with its structural conformation, allows for hydroxylation with the attached substrate. This molecule carries out important functions and is not species or sex specific. | This molecule has a heme which is bound to iron, which, combined with its structural conformation, allows for hydroxylation with the attached substrate. This molecule carries out important functions and is not species or sex specific. | ||
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<scene name='48/483888/Heme_group/3'>Heme_Group</scene> | <scene name='48/483888/Heme_group/3'>Heme_Group</scene> | ||
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==Quiz Question 1== | ==Quiz Question 1== | ||
(merely an example of what this section might look like) | (merely an example of what this section might look like) | ||
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| - | + | rom <scene name='48/483888/This_orientation/1'>this orientation</scene> can you identify the green, red, and blue parts of the molecule? | |
==See Also== | ==See Also== | ||
Revision as of 22:11, 2 March 2016
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Vitamin D activation by cytochrome P450, rickets (3c6g)[1]
by Isabel Hand, Elizabeth Humble, Kati Johnson, Samantha Kriksceonaitis, and Matthew Tiller
Student Projects for UMass Chemistry 423 Spring 2016
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