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==Structure== | ==Structure== | ||
disulphides, secondary, etc. | disulphides, secondary, etc. | ||
| - | <ref name=" | + | <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:
More help: Help:Editing |
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| 1kar, resolution 2.10Å () | |||||||||
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| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Gene: | HISD (Escherichia coli) | ||||||||
| Activity: | Histidinol dehydrogenase, with EC number 1.1.1.23 | ||||||||
| Related: | 1k75, 1kae, 1kah | ||||||||
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| 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].
|
[1].
Structure
disulphides, secondary, etc. [2]
Function
evolutionary purpose?
References
- ↑ 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
- ↑ Fallone CA. Epidemiology of the antibiotic resistance of Helicobacter pylori in Canada. Can J Gastroenterol. 2000 Nov;14(10):879-82. PMID:11111111

