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.

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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

L-Histidinol Dehydrogenase

The enzyme l-histidinol dehydrogenase (HisD)

ALL INFORMATION IN HERE!!! sub-headings for topics of interest (mechanism, binding sites, etc.) Basic information, current knowledge of areas found, etc. Structural

Overall Structure

HisD is a homodimer, with each subunit consisting of a globule segment, and an extending tail. The two larger domains (1 and 2) are within the globule, and domains 3 and 4 are found in the tail.

Beta Sheets

alpha helices

Other information??

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