1HOE

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

Summary for 1HOE

Entry DOI	10.2210/pdb1hoe/pdb
Descriptor	ALPHA-AMYLASE INHIBITOR (2 entities in total)
Functional Keywords	glycosidase inhibitor
Biological source	Streptomyces tendae
Total number of polymer chains	1
Total formula weight	7967.74
Authors	Pflugrath, J.W.,Wiegand, G.,Huber, R. (deposition date: 1989-01-27, release date: 1989-04-19, Last modification date: 2024-11-06)
Primary citation	Pflugrath, J.W.,Wiegand, G.,Huber, R.,Vertesy, L. Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A. J.Mol.Biol., 189:383-386, 1986 Cited by PubMed Abstract: 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. PubMed: 3489104 DOI: 10.1016/0022-2836(86)90520-6 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation