1gct
From Proteopedia
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 20:41:31 2008
