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- | =='''Pantetheinase (4CYG)'''== | + | =='''Pantetheinase (4CYG)<ref>PMID: 25478849 </ref>'''== |
by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant] | by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant] | ||
Revision as of 15:55, 25 February 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
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The two protein subunits possess dense regions of
Overall Structure
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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.
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Additional Features
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Quiz Question 1
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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
- ↑ 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