1gct

From Proteopedia

Revision as of 13:49, 20 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search
Image:1gct.gif

1gct, resolution 1.6Å

Drag the structure with the mouse to rotate

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] with SO4 as ligand. Active as Chymotrypsin, with EC number 3.4.21.1 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 Tue Nov 20 15:57:03 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gct"
Personal tools