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==Structure==
==Structure==
disulphides, secondary, etc.
disulphides, secondary, etc.
-
<ref name="superseconday"> PMID: </ref>
+
<ref name="supersecondary"> PMID:11111111 </ref>

Revision as of 21:51, 2 April 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 1kar

Drag the structure with the mouse to rotate
1kar, resolution 2.10Å ()
Ligands: ,
Non-Standard Residues:
Gene: HISD (Escherichia coli)
Activity: Histidinol dehydrogenase, with EC number 1.1.1.23
Related: 1k75, 1kae, 1kah
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

My Protein of Interest (MPI)

Basic information, current knowledge of areas found, etc.

Picture

Sec structure [1].

Insert caption here

Drag the structure with the mouse to rotate

[1].

Structure

disulphides, secondary, etc. [2]


Function

evolutionary purpose?


References

  1. 1.0 1.1 Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:11842181 doi:10.1073/pnas.022476199
  2. Fallone CA. Epidemiology of the antibiotic resistance of Helicobacter pylori in Canada. Can J Gastroenterol. 2000 Nov;14(10):879-82. PMID:11111111
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