1hoe

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Image:1hoe.gif

1hoe, resolution 2.0Å

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CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A

Overview

The crystal and molecular structure of the alpha-amylase inhibitor Hoe-467A has been determined and refined at high resolution. The polypeptide chain is folded in two triple-stranded sheets, which form a barrel. The topology of folding is as found in the immunoglobulin domains. The amino acid triplet Trp18-Arg19-Tyr20 has an exceptional conformation and position in the molecule and is possibly involved in inhibitory activity.

About this Structure

1HOE is a Single protein structure of sequence from Streptomyces tendae. Full crystallographic information is available from OCA.

Reference

Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A., Pflugrath JW, Wiegand G, Huber R, Vertesy L, J Mol Biol. 1986 May 20;189(2):383-6. PMID:3489104

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