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

Summary for 2D2O

• Entry DOI: 10.2210/pdb2d2o/pdb
• Related: 1VFK 1VFM 1VFO 1VFU
• Related PRD ID: PRD_900035
• Descriptor: 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, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: beta/alpha barrel, hydrolase
• Biological source: Thermoactinomyces vulgaris
• Total number of polymer chains: 2
• Total formula weight: 137168.13

Authors

Ohtaki, A.,Mizuno, M.,Yoshida, H.,Tonozuka, T.,Sakano, Y.,Kamitori, S. (deposition date: 2005-09-13, release date: 2006-08-29, Last modification date: 2021-11-10)

• Primary citation: Ohtaki, A.,Mizuno, M.,Yoshida, H.,Tonozuka, T.,Sakano, Y.,Kamitori, S.; 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., 341:1041-1046, 2006; PubMed: 16564038; DOI: 10.1016/j.carres.2006.01.029

Experimental method

X-RAY DIFFRACTION (2.1 Å)