2K46
 
 | | Xenopus laevis malectin complexed with nigerose (Glcalpha1-3Glc) | | 分子名称: | MGC80075 protein, alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose | | 著者 | Schallus, T. | | 登録日 | 2008-05-28 | | 公開日 | 2008-08-12 | | 最終更新日 | 2024-05-01 | | 実験手法 | SOLUTION NMR | | 主引用文献 | Malectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein N-Glycosylation
Mol.Cell.Biol., 19, 2008
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5DKZ
 | | Crystal structure of glucosidase II alpha subunit (alpha3-Glc2-bound from) | | 分子名称: | Alpha glucosidase-like protein, alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose | | 著者 | Satoh, T, Toshimori, T, Yan, G, Yamaguchi, T, Kato, K. | | 登録日 | 2015-09-04 | | 公開日 | 2016-01-27 | | 最終更新日 | 2020-07-29 | | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | | 主引用文献 | Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.
Sci Rep, 6, 2016
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5MAN
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6K0N
 | | Catalytic domain of GH87 alpha-1,3-glucanase in complex with nigerose | | 分子名称: | ACETIC ACID, Alpha-1,3-glucanase, CALCIUM ION, ... | | 著者 | Itoh, T, Intuy, R, Suyotha, W, Hayashi, J, Yano, S, Makabe, K, Wakayama, M, Hibi, T. | | 登録日 | 2019-05-07 | | 公開日 | 2019-12-25 | | 最終更新日 | 2023-11-22 | | 実験手法 | X-RAY DIFFRACTION (1.6 Å) | | 主引用文献 | Structural insights into substrate recognition and catalysis by glycoside hydrolase family 87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11.
Febs J., 287, 2020
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6K0P
 | | Catalytic domain of GH87 alpha-1,3-glucanase D1045A in complex with nigerose | | 分子名称: | ACETIC ACID, Alpha-1,3-glucanase, CALCIUM ION, ... | | 著者 | Itoh, T, Intuy, R, Suyotha, W, Hayashi, J, Yano, S, Makabe, K, Wakayama, M, Hibi, T. | | 登録日 | 2019-05-07 | | 公開日 | 2019-12-25 | | 最終更新日 | 2023-11-22 | | 実験手法 | X-RAY DIFFRACTION (1.424 Å) | | 主引用文献 | Structural insights into substrate recognition and catalysis by glycoside hydrolase family 87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11.
Febs J., 287, 2020
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6K0Q
 | | Catalytic domain of GH87 alpha-1,3-glucanase D1068A in complex with nigerose | | 分子名称: | ACETIC ACID, Alpha-1,3-glucanase, CALCIUM ION, ... | | 著者 | Itoh, T, Intuy, R, Suyotha, W, Hayashi, J, Yano, S, Makabe, K, Wakayama, M, Hibi, T. | | 登録日 | 2019-05-07 | | 公開日 | 2019-12-25 | | 最終更新日 | 2023-11-22 | | 実験手法 | X-RAY DIFFRACTION (1.564 Å) | | 主引用文献 | Structural insights into substrate recognition and catalysis by glycoside hydrolase family 87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11.
Febs J., 287, 2020
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6K0S
 | | Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with nigerose | | 分子名称: | ACETIC ACID, Alpha-1,3-glucanase, CALCIUM ION, ... | | 著者 | Itoh, T, Intuy, R, Suyotha, W, Hayashi, J, Yano, S, Makabe, K, Wakayama, M, Hibi, T. | | 登録日 | 2019-05-07 | | 公開日 | 2019-12-25 | | 最終更新日 | 2023-11-22 | | 実験手法 | X-RAY DIFFRACTION (1.534 Å) | | 主引用文献 | Structural insights into substrate recognition and catalysis by glycoside hydrolase family 87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11.
Febs J., 287, 2020
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6K0V
 | | Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides | | 分子名称: | Alpha-1,3-glucanase, CALCIUM ION, SULFATE ION, ... | | 著者 | Itoh, T, Intuy, R, Suyotha, W, Hayashi, J, Yano, S, Makabe, K, Wakayama, M, Hibi, T. | | 登録日 | 2019-05-07 | | 公開日 | 2019-12-25 | | 最終更新日 | 2023-11-22 | | 実験手法 | X-RAY DIFFRACTION (2.504 Å) | | 主引用文献 | Structural insights into substrate recognition and catalysis by glycoside hydrolase family 87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11.
Febs J., 287, 2020
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7WJC
 | | Crystal structure of Lactococcus lactis subsp. cremoris GH31 alpha-1,3-glucosidase mutant D394A in complex with nigerose | | 分子名称: | 1,2-ETHANEDIOL, Alpha-xylosidase, alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose | | 著者 | Ikegaya, M, Miyazaki, T. | | 登録日 | 2022-01-06 | | 公開日 | 2022-03-30 | | 最終更新日 | 2023-11-29 | | 実験手法 | X-RAY DIFFRACTION (1.75 Å) | | 主引用文献 | Structural basis of the strict specificity of a bacterial GH31 alpha-1,3-glucosidase for nigerooligosaccharides.
J.Biol.Chem., 298, 2022
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