1sbw

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Revision as of 00:08, 21 November 2007

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spinqualitylabelsall models 1sbw, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF MUNG BEAN INHIBITOR LYSINE ACTIVE FRAGMENT COMPLEX WITH BOVINE BETA-TRYPSIN AT 1.8A RESOLUTION

Overview

The crystal structure of the complex of mung bean inhibitor lysine active, fragment with bovine beta-trypsin has been determined by X-ray, crystallographic analysis at a resolution of 1.8 A. Refinement of the, model of the complex converged at a final R value of 0.16. From the, resulting electron density map, about one-third of the residues of the, inhibitor were identified and two residues, at position P4 and P2', respectively, were found to be inconsistent with the sequence reported, previously. The peptide chain of the inhibitor at the trypsin active site, turns back sharply at Pro23I and forms a 9-residue reactive loop, which, interacts with trypsin in a similar manner to the other families of, inhibitors, suggesting an important and common role of these regions in, exhibiting inhibitory activity.

About this Structure

1SBW is a Protein complex structure of sequences from Bos taurus and Vigna radiata with CA and SO4 as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8A resolution., Zhu Y, Huang Q, Chi C, J Biomol Struct Dyn. 1999 Jun;16(6):1219-24. PMID:10447205

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