2D2O
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![BU of 2d2o by Molmil](/molmil-images/mine/2d2o) | 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
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