3gch
From Proteopedia
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| - | [[Image:3gch.gif|left|200px]] | + | [[Image:3gch.gif|left|200px]] |
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| - | '''CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN''' | + | {{Structure |
| + | |PDB= 3gch |SIZE=350|CAPTION= <scene name='initialview01'>3gch</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=OAC:TRANS-O-HYDROXY-ALPHA-METHYL CINNAMATE'>OAC</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3GCH is a [ | + | 3GCH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GCH OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and activity of two photoreversible cinnamates bound to chymotrypsin., Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 May 22;29(20):4871-9. PMID:[http:// | + | Structure and activity of two photoreversible cinnamates bound to chymotrypsin., Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 May 22;29(20):4871-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2364065 2364065] |
[[Category: Chymotrypsin]] | [[Category: Chymotrypsin]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:04:57 2008'' |
Revision as of 17:04, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN
Overview
The serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation.
About this Structure
3GCH is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure and activity of two photoreversible cinnamates bound to chymotrypsin., Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 May 22;29(20):4871-9. PMID:2364065
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