Stancu Harmon Tiedman Sandbox 12
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(New page: ==The Mechanism of Trypsin== The structure of trypsin is characterized by an active site with a catalytic triad His- Asp- Ser (residue numbers 57, 102 and 195). The His 57 acts as a proton...)
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Revision as of 14:46, 19 February 2010
The Mechanism of Trypsin
The structure of trypsin is characterized by an active site with a catalytic triad His- Asp- Ser (residue numbers 57, 102 and 195). The His 57 acts as a proton acceptor for the Ser 195, activating the nucleophilic attack at the carbonyl group on incident proteins. Asp 102 further stabilizes the histidine residue through hydrogen bonding. The specificity of the active site pocket is characterized by the presence of an anionic Asp residue, 189, used to create ionic interactions to accommodate bulky side chains like Arg and Lys from the other protein
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| 3cin, resolution 1.70Å () | |||||||||
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| Ligands: | , , | ||||||||
| Gene: | TM1419, TM_1419 (Thermotoga maritima MSB8) | ||||||||
| Activity: | Inositol-3-phosphate synthase, with EC number 5.5.1.4 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
