Sandbox Reserved 328

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

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D load='1kar' size='350' frame='false' scene=
1kar, resolution 2.10Å (default scene)
Ligands:	HSM, ZN
Non-Standard Residues:	MSE
Gene:	HISD (Escherichia coli)
Activity:	Histidinol dehydrogenase, with EC number 1.1.1.23
Related:	1k75, 1kae, 1kah
Structural annotation: Resources: CATH : 1Kara02, 1Kara01, 1Karb01, 1Karb02 InterPro : Ipr012131, Ipr001692 Pfam : PF00815 SCOP : d1kara_, d1karb_ UniProt : P06988
Functional annotation: Biological process: histidine biosynthetic process amino acid biosynthetic process Molecular function: metal ion binding NAD binding histidinol dehydrogenase activity oxidoreductase activity zinc ion binding
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

My Protein of Interest (MPI)

Basic information, current knowledge of areas found, etc.

Picture

Sec structure .

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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Structure

disulphides, secondary, etc.

Function

evolutionary purpose?