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1BLI

BACILLUS LICHENIFORMIS ALPHA-AMYLASE

1BLI の概要
エントリーDOI10.2210/pdb1bli/pdb
分子名称ALPHA-AMYLASE, CALCIUM ION, SODIUM ION, ... (4 entities in total)
機能のキーワードhydrolase, glycosyltransferase, alpha-amylase, starch degradation, alpha-1, 4-glucan-4-glucanohydrolase, thermostability, calcium, sodium
由来する生物種Bacillus licheniformis
タンパク質・核酸の鎖数1
化学式量合計55410.18
構造登録者
Machius, M.,Declerck, N.,Huber, R.,Wiegand, G. (登録日: 1998-01-07, 公開日: 1999-03-23, 最終更新日: 2024-05-22)
主引用文献Machius, M.,Declerck, N.,Huber, R.,Wiegand, G.
Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad.
Structure, 6:281-292, 1998
Cited by
PubMed Abstract: The structural basis as to how metals regulate the functional state of a protein by altering or stabilizing its conformation has been characterized in relatively few cases because the metal-free form of the protein is often partially disordered and unsuitable for crystallographic analysis. This is not the case, however, for Bacillus licheniformis alpha-amylase (BLA) for which the structure of the metal-free form is available. BLA is a hyperthermostable enzyme which is widely used in biotechnology, for example in the breakdown of starch or as a component of detergents. The determination of the structure of BLA in the metal-containing form, together with comparisons to the apo enzyme, will help us to understand the way in which metal ions can regulate enzyme activity.
PubMed: 9551551
DOI: 10.1016/S0969-2126(98)00032-X
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 1bli
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2026-02-04に公開中

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