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Revision as of 17:56, 7 January 2014
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. This reservation includes Sandbox Reserved 440 through Sandbox Reserved 450 and Sandbox Reserved 835 through Sandbox Reserved 894. |
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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. There is a hydrophobic binding pocket to help align the 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
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2agi, resolution 1.14Å () | |||||||||
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Ligands: | , | ||||||||
Non-Standard Residues: | , | ||||||||
Activity: | Trypsin, with EC number 3.4.21.4 | ||||||||
Related: | 2age, 2agg, 2ah4 | ||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |