Template:Sandbox Reserved Taylor 1

From Proteopedia

Revision as of 04:48, 8 February 2014 by Ann Taylor (Talk | contribs)
Jump to: navigation, search
This Sandbox is Reserved from Jan 1, through May 1, 2014 for use in a Biochemistry course taught by Ann Taylor at the University of Tennessee, Knoxville, USA. -->
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

Trypsin: an example of a serine protease

Trypsin is a serine protease. It works with a catalytic triad of aspartic acid, histidine and serine to catalyze the formation of a covalent intermediate with the substrate. This structure shows the binding of trypsin to a competitive inhibitor, leupeptin. There is a hydrophobic binding pocket to help align the substrate protein with the enzyme, and an oxyanion hole to stabilize the intermediate. Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277



PDB ID 2agi

Drag the structure with the mouse to rotate
2agi, resolution 1.14Å ()
Ligands: ,
Non-Standard Residues: ,
Activity: Trypsin, with EC number 3.4.21.4
Related: 2age, 2agg, 2ah4
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Retrieved from "http://52.214.119.220/wiki/index.php/Template:Sandbox_Reserved_Taylor_1"
Personal tools