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: 2024-05-29) |
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 Cited by PubMed: 16564038DOI: 10.1016/j.carres.2006.01.029 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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