8C0Z
| CryoEM structure of a tungsten-containing aldehyde oxidoreductase from Aromatoleum aromaticum | 分子名称: | Aldehyde:ferredoxin oxidoreductase,tungsten-containing, BENZOIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, ... | 著者 | Winiarska, A, Ramirez-Amador, F, Hege, D, Gemmecker, Y, Prinz, S, Hochberg, G, Heider, J, Szaleniec, M, Schuller, J.M. | 登録日 | 2022-12-19 | 公開日 | 2023-05-31 | 最終更新日 | 2024-07-24 | 実験手法 | ELECTRON MICROSCOPY (3.22 Å) | 主引用文献 | A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire. Sci Adv, 9, 2023
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6X1O
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6X6U
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1B25
| FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS | 分子名称: | IRON/SULFUR CLUSTER, PROTEIN (FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE), TUNGSTOPTERIN | 著者 | Hu, Y.L, Faham, S, Roy, R, Adams, M.W.W, Rees, D.C. | 登録日 | 1998-12-04 | 公開日 | 1999-03-24 | 最終更新日 | 2023-08-09 | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | 主引用文献 | Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications. J.Mol.Biol., 286, 1999
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1B4N
| FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS, COMPLEXED WITH GLUTARATE | 分子名称: | CALCIUM ION, FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE, GLUTARIC ACID, ... | 著者 | Hu, Y.L, Faham, S, Roy, R, Adams, M.W.W, Rees, D.C. | 登録日 | 1998-12-24 | 公開日 | 1999-05-18 | 最終更新日 | 2024-05-22 | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | 主引用文献 | Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications. J.Mol.Biol., 286, 1999
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1AOR
| STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE | 分子名称: | ALDEHYDE FERREDOXIN OXIDOREDUCTASE, FE (III) ION, IRON/SULFUR CLUSTER, ... | 著者 | Chan, M.K, Mukund, S, Kletzin, A, Adams, M.W.W, Rees, D.C. | 登録日 | 1995-02-13 | 公開日 | 1995-04-20 | 最終更新日 | 2024-02-07 | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | 主引用文献 | Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science, 267, 1995
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4Z3Z
| Active site complex BamBC of Benzoyl Coenzyme A reductase in complex with Zinc | 分子名称: | Benzoyl-CoA reductase, putative, IRON/SULFUR CLUSTER, ... | 著者 | Weinert, T, Kung, J.W, Weidenweber, S, Huwiler, S.G, Boll, M, Ermler, U. | 登録日 | 2015-04-01 | 公開日 | 2015-06-24 | 最終更新日 | 2024-01-10 | 実験手法 | X-RAY DIFFRACTION (2.666 Å) | 主引用文献 | Structural basis of enzymatic benzene ring reduction. Nat.Chem.Biol., 11, 2015
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4Z3Y
| Active site complex BamBC of Benzoyl Coenzyme A reductase in complex with Benzoyl-CoA | 分子名称: | Benzoyl-CoA reductase, putative, IRON/SULFUR CLUSTER, ... | 著者 | Weinert, T, Kung, J.W, Weidenweber, S, Huwiler, S.G, Boll, M, Ermler, U. | 登録日 | 2015-04-01 | 公開日 | 2015-07-01 | 最終更新日 | 2024-01-10 | 実験手法 | X-RAY DIFFRACTION (2.359 Å) | 主引用文献 | Structural basis of enzymatic benzene ring reduction. Nat.Chem.Biol., 11, 2015
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4Z3W
| Active site complex BamBC of Benzoyl Coenzyme A reductase in complex with 1,5 Dienoyl-CoA | 分子名称: | 1,5 Dienoyl-CoA, Benzoyl-CoA reductase, putative, ... | 著者 | Weinert, T, Kung, J, Weidenweber, S, Huwiler, S, Boll, M, Ermler, U. | 登録日 | 2015-04-01 | 公開日 | 2015-06-24 | 最終更新日 | 2024-01-10 | 実験手法 | X-RAY DIFFRACTION (2.208 Å) | 主引用文献 | Structural basis of enzymatic benzene ring reduction. Nat.Chem.Biol., 11, 2015
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4Z3X
| Active site complex BamBC of Benzoyl Coenzyme A reductase in complex with 1-Monoenoyl-CoA | 分子名称: | 1,5 Dienoyl-CoA, Benzoyl-CoA reductase, putative, ... | 著者 | Weinert, T, Kung, J.W, Weidenweber, S, Huwiler, S.G, Boll, M, Ermler, U. | 登録日 | 2015-04-01 | 公開日 | 2015-06-24 | 最終更新日 | 2024-01-10 | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | 主引用文献 | Structural basis of enzymatic benzene ring reduction. Nat.Chem.Biol., 11, 2015
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4Z40
| Active site complex BamBC of Benzoyl Coenzyme A reductase as isolated | 分子名称: | Benzoyl-CoA reductase, putative, IRON/SULFUR CLUSTER, ... | 著者 | Weinert, T, Kung, J.W, Weidenweber, S, Huwiler, S.G, Boll, M, Ermler, U. | 登録日 | 2015-04-01 | 公開日 | 2015-06-24 | 最終更新日 | 2024-01-10 | 実験手法 | X-RAY DIFFRACTION (2.35 Å) | 主引用文献 | Structural basis of enzymatic benzene ring reduction. Nat.Chem.Biol., 11, 2015
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