Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft

Protein Data Bank Japan2024-05-29 更新2026-03-21 收录

酶结构解析

底物结合

数据链接：

https://pdbj.org/mine/summary/2d2o 数据链接链接失效反馈

官方服务：

资源简介：

Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft Descriptor: CALCIUM ION, Neopullulanase 2, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose Authors: Ohtaki, A, Mizuno, M, Yoshida, H, Tonozuka, T, Sakano, Y, Kamitori, S. Deposit date: 2005-09-13 Release date: 2006-08-29 Last modified: 2024-05-29 Method: X-RAY DIFFRACTION (2.1 Å) Cite: Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft Carbohydr.Res., 341, 2006

创建时间：

2005-09-13

Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft

资源简介：

相关数据集