1SBP
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![BU of 1sbp by Molmil](/molmil-images/mine/1sbp) | |
3WU6
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![BU of 3wu6 by Molmil](/molmil-images/mine/3wu6) | Oxidized E.coli Lon Proteolytic domain | Descriptor: | Lon protease, SULFATE ION | Authors: | Nishii, W, Kukimoto-Niino, M, Terada, T, Shirouzu, M, Muramatsu, T, Yokoyama, S. | Deposit date: | 2014-04-22 | Release date: | 2014-11-12 | Last modified: | 2023-11-08 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis. Nat. Chem. Biol., 11, 2015
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3WU5
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![BU of 3wu5 by Molmil](/molmil-images/mine/3wu5) | Reduced E.coli Lon Proteolytic domain | Descriptor: | Lon protease, SULFATE ION | Authors: | Nishii, W, Kukimoto-Niino, M, Terada, T, Shirouzu, M, Muramatsu, T, Yokoyama, S. | Deposit date: | 2014-04-22 | Release date: | 2014-11-12 | Last modified: | 2023-11-08 | Method: | X-RAY DIFFRACTION (2.07 Å) | Cite: | A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis. Nat. Chem. Biol., 11, 2015
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3WU3
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![BU of 3wu3 by Molmil](/molmil-images/mine/3wu3) | Reduced-form structure of E.coli Lon Proteolytic domain | Descriptor: | Lon protease, SULFATE ION | Authors: | Nishii, W, Kukimoto-Niino, M, Terada, T, Shirouzu, M, Muramatsu, T, Yokoyama, S. | Deposit date: | 2014-04-22 | Release date: | 2014-11-12 | Last modified: | 2023-11-08 | Method: | X-RAY DIFFRACTION (1.82 Å) | Cite: | A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis. Nat. Chem. Biol., 11, 2015
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1C53
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![BU of 1c53 by Molmil](/molmil-images/mine/1c53) | S-CLASS CYTOCHROMES C HAVE A VARIETY OF FOLDING PATTERNS: STRUCTURE OF CYTOCHROME C-553 FROM DESULFOVIBRIO VULGARIS DETERMINED BY THE MULTI-WAVELENGTH ANOMALOUS DISPERSION METHOD | Descriptor: | CYTOCHROME C553, PROTOPORPHYRIN IX CONTAINING FE | Authors: | Nakagawa, A, Higuchi, Y, Yasuoka, N, Katsube, Y, Yaga, T. | Deposit date: | 1991-08-26 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method. J.Biochem.(Tokyo), 108, 1990
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