Sandbox Reserved 338

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<scene name='Sandbox_Reserved_338/2vnc/3'>Test scene</scene>
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there is a glutamate residue, <scene name='Sandbox_Reserved_338/2vnc/3'>residue 100</scene> that I am interested in showing.
==References==
==References==
<references/>
<references/>

Revision as of 19:21, 15 March 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


PDB ID 2vnc

Drag the structure with the mouse to rotate
2vnc, resolution 3.00Å ()
Related: 2vuy, 2vr5, 2vnb
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



A debranching enzyme is responsible for the breakdown of glycogen [1]. There are two main groups of debranching enzymes, and they are separated according to their activity [1]. The first group, consisting of pullulanase and isoamylases which only possess one function α-1,6-glycosidase activity [1]. Whereas the second group consists of glycogen debranching enzymes which possess two functions, both α-1,6-glycosidase and α-1,4-transferase activity [1].


there is a glutamate residue, that I am interested in showing.

References

  1. 1.0 1.1 1.2 1.3 Woo EJ, Lee S, Cha H, Park JT, Yoon SM, Song HN, Park KH. Structural insight into the bifunctional mechanism of the glycogen-debranching enzyme TreX from the archaeon Sulfolobus solfataricus. J Biol Chem. 2008 Oct 17;283(42):28641-8. Epub 2008 Aug 14. PMID:18703518 doi:10.1074/jbc.M802560200
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