3AUS
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3AUT
| Crystal structure of Bacillus megaterium glucose dehydrogenase 4 in complex with NADH | Descriptor: | 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, Glucose 1-dehydrogenase 4 | Authors: | Nishioka, T, Yasutake, Y, Nishiya, Y, Tamura, T. | Deposit date: | 2011-02-16 | Release date: | 2012-02-22 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure-guided mutagenesis for the improvement of substrate specificity of Bacillus megaterium glucose 1-dehydrogenase IV Febs J., 279, 2012
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3AY7
| Crystal structure of Bacillus megaterium glucose dehydrogenase 4 G259A mutant | Descriptor: | CHLORIDE ION, Glucose 1-dehydrogenase 4 | Authors: | Nishioka, T, Yasutake, Y, Nishiya, Y, Tamura, T. | Deposit date: | 2011-04-29 | Release date: | 2012-05-23 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structure-guided mutagenesis for the improvement of substrate specificity of Bacillus megaterium glucose 1-dehydrogenase IV Febs J., 279, 2012
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2ZK7
| Structure of a C-terminal deletion mutant of Thermoplasma acidophilum aldohexose dehydrogenase (AldT) | Descriptor: | Glucose 1-dehydrogenase related protein | Authors: | Nishioka, T, Yasutake, Y, Nishiya, Y, Tamura, N, Tamura, T. | Deposit date: | 2008-03-12 | Release date: | 2009-01-13 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (2.71 Å) | Cite: | C-terminal tail derived from the neighboring subunit is critical for the activity of Thermoplasma acidophilum D-aldohexose dehydrogenase Proteins, 74, 2009
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5B40
| The nucleosome structure containing H2B-K120 and H4-K31 monoubiquitinations | Descriptor: | DNA (146-MER), Histone H2A type 1-B/E, Histone H2B type 1-J, ... | Authors: | Machida, S, Sekine, S, Nishiyama, Y, Horikoshi, N, Kurumizaka, H. | Deposit date: | 2016-03-22 | Release date: | 2016-06-22 | Last modified: | 2023-11-08 | Method: | X-RAY DIFFRACTION (3.33 Å) | Cite: | Monoubiquitination of histones H2B and H4 changes the nucleosome stability without affecting the nucleosome structure To Be Published
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