1WVE
| p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 4-cresol dehydrogenase [hydroxylating] cytochrome c subunit, 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit, ... | 著者 | Cunane, L.M, Chen, Z.-W, McIntire, W.S, Mathews, F.S. | 登録日 | 2004-12-15 | 公開日 | 2005-03-08 | 最終更新日 | 2024-10-23 | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | 主引用文献 | p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon Its Binding to the Cytochrome Subunit Biochemistry, 44, 2005
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1WVF
| p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit | 分子名称: | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit, ACETIC ACID, CHLORIDE ION, ... | 著者 | Cunane, L.M, Chen, Z.-W, McIntire, W.S, Mathews, F.S. | 登録日 | 2004-12-15 | 公開日 | 2005-03-08 | 最終更新日 | 2024-10-09 | 実験手法 | X-RAY DIFFRACTION (1.3 Å) | 主引用文献 | p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon Its Binding to the Cytochrome Subunit Biochemistry, 44, 2005
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1DIQ
| CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE WITH SUBSTRATE BOUND | 分子名称: | CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, HEME C, ... | 著者 | Cunane, L.M, Chen, Z.W, Shamala, N, Mathews, F.S, Cronin, C.S, McIntire, W.S. | 登録日 | 1999-11-29 | 公開日 | 1999-12-08 | 最終更新日 | 2024-10-30 | 実験手法 | X-RAY DIFFRACTION (2.75 Å) | 主引用文献 | Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism. J.Mol.Biol., 295, 2000
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1DII
| CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION | 分子名称: | CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, HEME C, ... | 著者 | Cunane, L.M, Chen, Z.W, Shamala, N, Mathews, F.S, Cronin, C.N, McIntire, W.S. | 登録日 | 1999-11-29 | 公開日 | 1999-12-08 | 最終更新日 | 2021-03-03 | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | 主引用文献 | Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism. J.Mol.Biol., 295, 2000
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