This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Sandbox Reserved 328

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
{{STRUCTURE_1kar| PDB=1kar | SCENE= }}
{{STRUCTURE_1kar| PDB=1kar | SCENE= }}
=L-Histidinol Dehydrogenase=
=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.
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 <scene name='Globule Domains'>(1 and 2)</scene>. are within the globule, and domains 3 and 4 are found in the tail.
==Enzymatic mechanism==
==Enzymatic mechanism==
Line 10: Line 15:
==Other information??==
==Other information??==
-
Sec structure <ref name="1kar" />.
+
<ref name="1kar" />.
-
<Structure load='XXXX' size='500' frame='true' align='RIGHT' caption='Insert caption here' scene='Insert optional scene name here' />
+
<ref name="1kar"> PMID:11842181 </ref>.
<ref name="1kar"> PMID:11842181 </ref>.
-
==Structure==
 
-
disulphides, secondary, etc.
 
-
<ref name="supersecondary"> PMID:11111111 </ref>
 
- 
- 
- 
-
==Function==
 
-
evolutionary purpose?
 
==References==
==References==
<references/>
<references/>

Revision as of 04:26, 3 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

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 . 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
Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_328"
Personal tools