Sandbox Reserved 338

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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.

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spinqualitylabelsall models PDB ID 2vnc Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2vnc, resolution 3.00Å ()
Related:	2vuy, 2vr5, 2vnb
Structural annotation: Resources: InterPro : Ipr017853, Ipr013780, Ipr015902, Ipr014756, Ipr013783, Ipr013781, Ipr011837, Ipr006047, Ipr004193 Pfam : PF00128, PF02922
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
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 pullulanases 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].

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