Sandbox Reserved 434: Difference between revisions
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[[Student Projects for UMass Chemistry 423 Spring 2016]] | [[Student Projects for UMass Chemistry 423 Spring 2016]] | ||
<StructureSection load='4CYG' size='350' side='right' caption='caption for Molecular Playground (PDB entry [[4CYG]])' scene=''> | |||
==Introduction== | ==Introduction== | ||
The two protein subunits possess dense regions of <scene name='48/483891/Secondary_structure/1'>beta strands and alpha helices.</scene> | The two protein subunits possess dense regions of <scene name='48/483891/Secondary_structure/1'>beta strands and alpha helices.</scene> | ||
Main points: | Main points: | ||
| Line 15: | Line 15: | ||
- A small paragraph on its discovery | - A small paragraph on its discovery | ||
- The broad impact of the protein (what happens if it loses function?) | - The broad impact of the protein (what happens if it loses function?) | ||
==Overall Structure== | ==Overall Structure== | ||
- 506 total residues, 87 missing | - 506 total residues, 87 missing | ||
- Two chains, each with many alpha helices and beta sheets | - Two chains, each with many alpha helices and beta sheets | ||
| Line 32: | Line 30: | ||
==Binding Interactions== | ==Binding Interactions== | ||
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<scene name='48/483891/Alpha_and_beta_structures/2'>Alpha and Beta Structures</scene> | <scene name='48/483891/Alpha_and_beta_structures/2'>Alpha and Beta Structures</scene> | ||
==Additional Features== | ==Additional Features== | ||
<scene name='48/483891/Polarity/1'>The purple chains represent the polar and therefore hydrophilic regions of 4CYG and the grey chains represent the nonpolar hydrophobic regions of 4CYG.</scene> | <scene name='48/483891/Polarity/1'>The purple chains represent the polar and therefore hydrophilic regions of 4CYG and the grey chains represent the nonpolar hydrophobic regions of 4CYG.</scene> | ||
==Quiz Question 1== | ==Quiz Question 1== | ||
- Additional research needed to formulate question (may potentially pertain to structure-substrate interaction) | - Additional research needed to formulate question (may potentially pertain to structure-substrate interaction) | ||
==See Also== | ==See Also== | ||
Revision as of 22:23, 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. |
Pantetheinase (4CYG)[1]
by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant]
Student Projects for UMass Chemistry 423 Spring 2016 <StructureSection load='4CYG' size='350' side='right' caption='caption for Molecular Playground (PDB entry 4CYG)' scene=>
Introduction
The two protein subunits possess dense regions of beta strands and alpha helices. Main points: - introduce general characteristics of protein (location within cell, substrate activity) - A small paragraph on its discovery - The broad impact of the protein (what happens if it loses function?)
Overall Structure
- 506 total residues, 87 missing - Two chains, each with many alpha helices and beta sheets - Chain A, colored by component 43 missing residues: 8-20, 484-513 - Chain B 44 missing residues: 8-20, 484-513
Ligands and non-standard residues - 2 RRV - 2 PEG - 8 NAG
Binding Interactions
Vanin-1 binds with 3 unique ligands including PEG (DI(HYDROXYETHYL)ETHER), NAG (N-ACETYL-D-GLUCOSAMINE) and RRV ((2R)-2,4-dihydroxy-N-[(3S)-3-hydroxy-4-phenylbutyl]-3,3-dimethylbutanamide). NAG and RRV both bind in the alpha helixes and beta strands but PEG only binds to the beta strands.
Additional Features
Quiz Question 1
- Additional research needed to formulate question (may potentially pertain to structure-substrate interaction)
See Also
Credits
Introduction - Patrick Tonne
Overall Structure - Luke Schnitzler
Drug Binding Site - Owen O'Connor
Additional Features - Nick Saint
Quiz Question 1 - Tyler Russell
References
- ↑ Boersma YL, Newman J, Adams TE, Cowieson N, Krippner G, Bozaoglu K, Peat TS. The structure of vanin 1: a key enzyme linking metabolic disease and inflammation. Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3320-9. doi:, 10.1107/S1399004714022767. Epub 2014 Nov 28. PMID:25478849 doi:https://dx.doi.org/10.1107/S1399004714022767
