4RLO
| Human p70s6k1 with ruthenium-based inhibitor EM5 | Descriptor: | CHLORIDE ION, DIMETHYL SULFOXIDE, GLYCEROL, ... | Authors: | Domsic, J.F, Barber-Rotenberg, J, Salami, J, Qin, J, Marmorstein, R. | Deposit date: | 2014-10-17 | Release date: | 2015-01-21 | Last modified: | 2023-09-20 | Method: | X-RAY DIFFRACTION (2.527 Å) | Cite: | Development of Organometallic S6K1 Inhibitors. J.Med.Chem., 58, 2015
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5WJD
| Crystal structure of Naa80 bound to acetyl-CoA | Descriptor: | ACETYL COENZYME *A, CG8481, isoform B, ... | Authors: | Goris, M, Magin, R.S, Marmorstein, R, Arnesen, T. | Deposit date: | 2017-07-21 | Release date: | 2018-03-28 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (2.001 Å) | Cite: | Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc. Natl. Acad. Sci. U.S.A., 115, 2018
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5WJE
| Crystal structure of Naa80 bound to a bisubstrate analogue | Descriptor: | Actin N-terminus peptide, CARBOXYMETHYL COENZYME *A, CG8481, ... | Authors: | Goris, M, Magin, R.S, Marmorstein, R, Arnesen, T. | Deposit date: | 2017-07-21 | Release date: | 2018-03-28 | Last modified: | 2023-10-04 | Method: | X-RAY DIFFRACTION (1.765 Å) | Cite: | Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc. Natl. Acad. Sci. U.S.A., 115, 2018
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7LJ9
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1YGH
| HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE | Descriptor: | GLYCEROL, PROTEIN (TRANSCRIPTIONAL ACTIVATOR GCN5) | Authors: | Trievel, R.C, Rojas, J.R, Sterner, D.E, Venkataramani, R, Wang, L, Zhou, J, Allis, C.D, Berger, S.L, Marmorstein, R. | Deposit date: | 1999-05-27 | Release date: | 1999-08-02 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc.Natl.Acad.Sci.USA, 96, 1999
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7RB3
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7RIG
| Structure of ACLY-D1026A-substrates | Descriptor: | (3S)-citryl-Coenzyme A, ADENOSINE-5'-DIPHOSPHATE, ATP-citrate synthase, ... | Authors: | Wei, X, Marmorstein, R. | Deposit date: | 2021-07-19 | Release date: | 2023-05-10 | Last modified: | 2023-05-31 | Method: | ELECTRON MICROSCOPY (2.2 Å) | Cite: | Allosteric role of the citrate synthase homology domain of ATP citrate lyase. Nat Commun, 14, 2023
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7RKZ
| Structure of ACLY D1026A-substrates-asym-int | Descriptor: | (3S)-citryl-Coenzyme A, ADENOSINE-5'-DIPHOSPHATE, ATP-citrate synthase, ... | Authors: | Wei, X, Marmorstein, R. | Deposit date: | 2021-07-22 | Release date: | 2023-05-10 | Method: | ELECTRON MICROSCOPY (2.6 Å) | Cite: | Allosteric role of the citrate synthase homology domain of ATP citrate lyase. Nat Commun, 14, 2023
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7RMP
| Structure of ACLY D1026A - substrates-asym | Descriptor: | (3S)-citryl-Coenzyme A, ADENOSINE-5'-DIPHOSPHATE, ATP-citrate synthase, ... | Authors: | Wei, X, Marmorstein, R. | Deposit date: | 2021-07-28 | Release date: | 2023-05-10 | Method: | ELECTRON MICROSCOPY (2.7 Å) | Cite: | Allosteric role of the citrate synthase homology domain of ATP citrate lyase. Nat Commun, 14, 2023
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7STX
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6C95
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6C9M
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6C9D
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8ETB
| the crystal structure of a rationally designed zinc sensor based on maltose binding protein - Zn binding conformation | Descriptor: | ACETATE ION, ZINC ION, Zinc Sensor protein | Authors: | Zhao, Z, Zhou, M, Zemerov, S.D, Marmorstein, R, Dmochowski, I.J. | Deposit date: | 2022-10-16 | Release date: | 2023-03-22 | Last modified: | 2023-04-19 | Method: | X-RAY DIFFRACTION (1.63 Å) | Cite: | Rational design of a genetically encoded NMR zinc sensor. Chem Sci, 14, 2023
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8F23
| The crystal structure of a rationally designed zinc sensor based on maltose binding protein - Apo conformation | Descriptor: | Zinc Sensor protein | Authors: | Zhao, Z, Zhou, M, Zemerov, S.d, Marmorstein, R, Dmochowski, I.J. | Deposit date: | 2022-11-06 | Release date: | 2023-03-22 | Last modified: | 2023-04-19 | Method: | X-RAY DIFFRACTION (1.93 Å) | Cite: | Rational design of a genetically encoded NMR zinc sensor. Chem Sci, 14, 2023
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8G1E
| Structure of ACLY-D1026A-products-asym | Descriptor: | (3S)-citryl-Coenzyme A, ACETYL COENZYME *A, ADENOSINE-5'-DIPHOSPHATE, ... | Authors: | Wei, X, Marmorstein, R. | Deposit date: | 2023-02-02 | Release date: | 2023-05-10 | Method: | ELECTRON MICROSCOPY (2.8 Å) | Cite: | Allosteric role of the citrate synthase homology domain of ATP citrate lyase. Nat Commun, 14, 2023
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8G5D
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8G0L
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8G1F
| Structure of ACLY-D1026A-products | Descriptor: | (3S)-citryl-Coenzyme A, ACETYL COENZYME *A, ADENOSINE-5'-DIPHOSPHATE, ... | Authors: | Wei, X, Marmorstein, R. | Deposit date: | 2023-02-02 | Release date: | 2023-05-10 | Method: | ELECTRON MICROSCOPY (2.4 Å) | Cite: | Allosteric role of the citrate synthase homology domain of ATP citrate lyase. Nat Commun, 14, 2023
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6O07
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3TOA
| Human MOF crystal structure with active site lysine partially acetylated | Descriptor: | 1,2-ETHANEDIOL, CHLORIDE ION, ZINC ION, ... | Authors: | Yuan, H, Ding, E.C, Marmorstein, R. | Deposit date: | 2011-09-04 | Release date: | 2011-11-09 | Last modified: | 2023-12-06 | Method: | X-RAY DIFFRACTION (3.004 Å) | Cite: | MYST protein acetyltransferase activity requires active site lysine autoacetylation. Embo J., 31, 2011
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3TO6
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3TO7
| Crystal structure of yeast Esa1 HAT domain bound to coenzyme A with active site lysine acetylated | Descriptor: | CACODYLIC ACID, COENZYME A, GLYCEROL, ... | Authors: | Yuan, H, Ding, E.C, Marmorstein, R. | Deposit date: | 2011-09-04 | Release date: | 2011-11-09 | Last modified: | 2023-12-06 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | MYST protein acetyltransferase activity requires active site lysine autoacetylation. Embo J., 31, 2011
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3TOB
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3TO9
| Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated | Descriptor: | 1,2-ETHANEDIOL, CACODYLIC ACID, COENZYME A, ... | Authors: | Yuan, H, Ding, E.C, Marmorstein, R. | Deposit date: | 2011-09-04 | Release date: | 2011-11-09 | Last modified: | 2012-01-18 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | MYST protein acetyltransferase activity requires active site lysine autoacetylation. Embo J., 31, 2011
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