8OPV
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![BU of 8opv by Molmil](/molmil-images/mine/8opv) | Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Resveratrol (Fragment-B-H11) | 分子名称: | 3-hydroxyacyl-CoA dehydrogenase, GLYCEROL, Putative acyltransferase Rv0859, ... | 著者 | Dalwani, S, Wierenga, R.K, Venkatesan, R. | 登録日 | 2023-04-10 | 公開日 | 2024-01-24 | 最終更新日 | 2024-08-14 | 実験手法 | X-RAY DIFFRACTION (2.8 Å) | 主引用文献 | Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate-channeling path between them. Acta Crystallogr D Struct Biol, 80, 2024
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8OQU
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![BU of 8oqu by Molmil](/molmil-images/mine/8oqu) | Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-92 | 分子名称: | 3-hydroxyacyl-CoA dehydrogenase, 4-chloranylbenzenesulfonic acid, GLYCEROL, ... | 著者 | Dalwani, S, Wierenga, R.K, Venkatesan, R. | 登録日 | 2023-04-12 | 公開日 | 2024-01-24 | 最終更新日 | 2024-08-14 | 実験手法 | X-RAY DIFFRACTION (2.89 Å) | 主引用文献 | Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate-channeling path between them. Acta Crystallogr D Struct Biol, 80, 2024
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8OQM
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![BU of 8oqm by Molmil](/molmil-images/mine/8oqm) | Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with Fragment-M-10 | 分子名称: | 3-hydroxyacyl-CoA dehydrogenase, 6-[(6-azanyl-4-oxidanyl-naphthalen-2-yl)sulfonylamino]-4-oxidanyl-naphthalene-2-sulfonic acid, 6-azanyl-4-oxidanyl-naphthalene-2-sulfonic acid, ... | 著者 | Dalwani, S, Wierenga, R.K, Venkatesan, R. | 登録日 | 2023-04-12 | 公開日 | 2024-01-24 | 最終更新日 | 2024-08-14 | 実験手法 | X-RAY DIFFRACTION (3.2 Å) | 主引用文献 | Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate-channeling path between them. Acta Crystallogr D Struct Biol, 80, 2024
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