1C7S
| BETA-N-ACETYLHEXOSAMINIDASE MUTANT D539A COMPLEXED WITH DI-N-ACETYL-BETA-D-GLUCOSAMINE (CHITOBIASE) | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, BETA-N-ACETYLHEXOSAMINIDASE, SULFATE ION | 著者 | Prag, G, Papanikolau, Y, Tavlas, G, Vorgias, C.E, Petratos, K, Oppenheim, A.B. | 登録日 | 2000-03-14 | 公開日 | 2000-09-20 | 最終更新日 | 2023-08-09 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540. J.Mol.Biol., 300, 2000
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1C7T
| BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE) | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, BETA-N-ACETYLHEXOSAMINIDASE, SULFATE ION | 著者 | Prag, G, Papanikolau, Y, Tavlas, G, Vorgias, C.E, Petratos, K, Oppenheim, A.B. | 登録日 | 2000-03-17 | 公開日 | 2000-09-20 | 最終更新日 | 2023-08-09 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540. J.Mol.Biol., 300, 2000
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1QBB
| BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHITOBIASE, SULFATE ION | 著者 | Tews, I, Perrakis, A, Oppenheim, A, Dauter, Z, Wilson, K.S, Vorgias, C.E. | 登録日 | 1996-06-07 | 公開日 | 1997-02-12 | 最終更新日 | 2023-08-09 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat.Struct.Biol., 3, 1996
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1QBA
| BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 | 分子名称: | CHITOBIASE, SULFATE ION | 著者 | Tews, I, Perrakis, A, Oppenheim, A, Dauter, Z, Wilson, K.S, Vorgias, C.E. | 登録日 | 1996-06-06 | 公開日 | 1997-01-11 | 最終更新日 | 2011-07-13 | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | 主引用文献 | Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat.Struct.Biol., 3, 1996
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