1gct: Difference between revisions
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[[Image:1gct.gif|left|200px]] | [[Image:1gct.gif|left|200px]] | ||
'''IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?''' | {{Structure | ||
|PDB= 1gct |SIZE=350|CAPTION= <scene name='initialview01'>1gct</scene>, resolution 1.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</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= | |||
}} | |||
'''IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GCT is a [ | 1GCT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCT OCA]. | ||
==Reference== | ==Reference== | ||
Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?, Dixon MM, Matthews BW, Biochemistry. 1989 Aug 22;28(17):7033-8. PMID:[http:// | Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?, Dixon MM, Matthews BW, Biochemistry. 1989 Aug 22;28(17):7033-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2819046 2819046] | ||
[[Category: Chymotrypsin]] | [[Category: Chymotrypsin]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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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 11:21:28 2008'' | ||
Revision as of 09:21, 20 March 2008
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| 1gct, resolution 1.6Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?
Overview
Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., & Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.
About this Structure
1GCT is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?, Dixon MM, Matthews BW, Biochemistry. 1989 Aug 22;28(17):7033-8. PMID:2819046
Page seeded by OCA on Thu Mar 20 11:21:28 2008
