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Sandbox Reserved 434

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Revision as of 15:55, 25 February 2016 by Lynmarie K Thompson (Talk | contribs)
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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

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The two protein subunits possess dense regions of



















Overall Structure

4cyg, insert caption here

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- 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

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Additional Features

pdbcode, Insert caption here

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Quiz Question 1

pdbcode, Insert caption here

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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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