1hoe
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| , resolution 2.0Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND THE MOLECULAR MODEL OF THE ALPHA-AMYLASE INHIBITOR HOE-467A
OverviewOverview
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 StructureAbout this Structure
1HOE is a Single protein structure of sequence from Streptomyces tendae. Full crystallographic information is available from OCA.
ReferenceReference
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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