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==Additional Features==
==Additional Features==
<Structure load='1a84' size='300' frame='true' align='right' caption='pdbcode, Insert caption here' scene='polarity' />
<Structure load='1a84' size='300' frame='true' align='right' caption='pdbcode, Insert caption here' scene='polarity' />
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<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>
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==Quiz Question 1==
==Quiz Question 1==

Revision as of 14:48, 1 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.


Contents

Pantetheinase (4CYG)[1]

by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant]

Student Projects for UMass Chemistry 423 Spring 2016

Introduction

4cyg, Insert caption here

Drag the structure with the mouse to rotate

The two protein subunits possess dense regions of 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

4cyg, insert caption here

Drag the structure with the mouse to rotate

- 506 total residues, 87 missing - Two chains, each with many alpha helices and beta sheets - 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.


4cyg, Insert caption here

Drag the structure with the mouse to rotate





















Additional Features

pdbcode, Insert caption here

Drag the structure with the mouse to rotate





















Quiz Question 1

pdbcode, Insert caption here

Drag the structure with the mouse to rotate





















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

  1. ↑ 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:http://dx.doi.org/10.1107/S1399004714022767
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