From Proteopedia

proteopedia linkproteopedia link

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 PDB ID 1kar Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
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
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

Contents 1 L-Histidinol Dehydrogenase 1.1 Overall Structure 1.2 Enzymatic mechanism 1.3 Other information?? 1.4 References

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.

Enzymatic mechanism

Other information??

^[1]. ^[1].

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