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1HX0

Structure of pig pancreatic alpha-amylase complexed with the "truncate" acarbose molecule (pseudotrisaccharide)

1HX0 の概要
エントリーDOI10.2210/pdb1hx0/pdb
関連するBIRD辞書のPRD_IDPRD_900001
分子名称ALPHA AMYLASE (PPA), 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (7 entities in total)
機能のキーワードalpha-amylase, inhibitor, carbohydrate, pancreas, hydrolase
由来する生物種Sus scrofa (pig)
タンパク質・核酸の鎖数1
化学式量合計57690.74
構造登録者
Qian, M.,Payan, F. (登録日: 2001-01-11, 公開日: 2001-08-08, 最終更新日: 2024-11-13)
主引用文献Qian, M.,Nahoum, V.,Bonicel, J.,Bischoff, H.,Henrissat, B.,Payan, F.
Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex
Biochemistry, 40:7700-7709, 2001
Cited by
PubMed Abstract: Mammalian alpha-amylases catalyze the hydrolysis of alpha-linked glucose polymers according to a complex processive mechanism. We have determined the X-ray structures of porcine pancreatic alpha-amylase complexes with the smallest molecule of the trestatin family (acarviosine-glucose) which inhibits porcine pancreatic alpha-amylase and yet is not hydrolyzed by the enzyme. A structure analysis at 1.38 A resolution of this complex allowed for a clear identification of a genuine single hexasaccharide species composed of two alpha-1,4-linked original molecules bound to the active site of the enzyme. The structural results supported by mass spectrometry experiments provide evidence for an enzymatically catalyzed condensation reaction in the crystal.
PubMed: 11412124
DOI: 10.1021/bi0102050
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.38 Å)
構造検証レポート
Validation report summary of 1hx0
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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