1MA3
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![BU of 1ma3 by Molmil](/molmil-images/mine/1ma3) | Structure of a Sir2 enzyme bound to an acetylated p53 peptide | Descriptor: | 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Cellular tumor antigen p53, Transcriptional regulatory protein, ... | Authors: | Avalos, J.L, Celic, I, Muhammad, S, Cosgrove, M.S, Boeke, J.D, Wolberger, C. | Deposit date: | 2002-07-31 | Release date: | 2002-10-16 | Last modified: | 2011-07-13 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure of a Sir2 enzyme bound to an acetylated p53 peptide Mol.Cell, 10, 2002
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1S7G
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![BU of 1s7g by Molmil](/molmil-images/mine/1s7g) | Structural Basis for the Mechanism and Regulation of Sir2 Enzymes | Descriptor: | 1,2-ETHANEDIOL, ADENOSINE-5-DIPHOSPHORIBOSE, HEXAETHYLENE GLYCOL, ... | Authors: | Avalos, J.L, Boeke, J.D, Wolberger, C. | Deposit date: | 2004-01-29 | Release date: | 2004-03-23 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Structural basis for the mechanism and regulation of sir2 enzymes Mol.Cell, 13, 2004
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7K6Q
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![BU of 7k6q by Molmil](/molmil-images/mine/7k6q) | Active state Dot1 bound to the H4K16ac nucleosome | Descriptor: | DNA (146-MER), Histone H2A type 1, Histone H2B 1.1, ... | Authors: | Valencia-Sanchez, M.I, De Ioannes, P.E, Miao, W, Truong, D.M, Lee, R, Armache, J.-P, Boeke, J.D, Armache, K.-J. | Deposit date: | 2020-09-21 | Release date: | 2021-02-10 | Method: | ELECTRON MICROSCOPY (3.1 Å) | Cite: | Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation. Science, 371, 2021
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7K6P
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![BU of 7k6p by Molmil](/molmil-images/mine/7k6p) | Active state Dot1 bound to the unacetylated H4 nucleosome | Descriptor: | DNA (146-MER), Histone H2A type 1, Histone H2B 1.1, ... | Authors: | Valencia-Sanchez, M.I, De Ioannes, P.E, Miao, W, Truong, D.M, Lee, R, Armache, J.-P, Boeke, J.D, Armache, K.-J. | Deposit date: | 2020-09-21 | Release date: | 2021-02-10 | Last modified: | 2024-03-06 | Method: | ELECTRON MICROSCOPY (3.2 Å) | Cite: | Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation. Science, 371, 2021
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