2TAA

STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A

「1TAA」から置き換えられました

2TAA の概要

• エントリーDOI: 10.2210/pdb2taa/pdb
• 分子名称: TAKA-AMYLASE A, CALCIUM ION (2 entities in total)
• 機能のキーワード: hydrolase (o-glycosyl)
• 由来する生物種: Aspergillus oryzae
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 157430.73

構造登録者

Kusunoki, M.,Matsuura, Y.,Tanaka, N.,Kakudo, M. (登録日: 1982-10-18, 公開日: 1982-10-21, 最終更新日: 2024-06-05)

主引用文献

Matsuura, Y.,Kusunoki, M.,Harada, W.,Kakudo, M.
Structure and possible catalytic residues of Taka-amylase A
J.Biochem.(Tokyo), 95:697-702, 1984

PubMed Abstract: A complete molecular model of Taka-amylase A consisting of 478 amino acid residues was built with the aid of amino acid sequence data. Some typical structural features of the molecule are described. A model fitting of an amylose chain in the catalytic site of the enzyme showed a possible productive binding mode between substrate and enzyme. On the basis of the difference Fourier analysis and the model fitting study, glutamic acid (Glu230) and aspartic acid (Asp297), which are located at the bottom of the cleft, were concluded to be the catalytic residues, serving as the general acid and base, respectively.

PubMed: 6609921

実験手法

X-RAY DIFFRACTION (3 Å)