1L74
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1L37
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1L56
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1D23
| THE STRUCTURE OF B-HELICAL C-G-A-T-C-G-A-T-C-G AND COMPARISON WITH C-C-A-A-C-G-T-T-G-G. THE EFFECT OF BASE PAIR REVERSALS | Descriptor: | DNA (5'-D(*CP*GP*AP*TP*CP*GP*AP*TP*CP*G)-3'), MAGNESIUM ION | Authors: | Grzeskowiak, K, Yanagi, K, Prive, G.G, Dickerson, R.E. | Deposit date: | 1991-05-29 | Release date: | 1991-10-15 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | The structure of B-helical C-G-A-T-C-G-A-T-C-G and comparison with C-C-A-A-C-G-T-T-G-G. The effect of base pair reversals. J.Biol.Chem., 266, 1991
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1L43
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1L61
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1L39
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1L62
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1L73
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1L53
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1L66
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1FDL
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1L36
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1L52
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6ICD
| REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE | Descriptor: | ISOCITRATE DEHYDROGENASE | Authors: | Hurley, J.H, Dean, A.M, Sohl, J.L, Koshlandjunior, D.E, Stroud, R.M. | Deposit date: | 1990-05-30 | Release date: | 1991-10-15 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Regulation of an enzyme by phosphorylation at the active site. Science, 249, 1990
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7ABP
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6EST
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1BBP
| MOLECULAR STRUCTURE OF THE BILIN BINDING PROTEIN (BBP) FROM PIERIS BRASSICAE AFTER REFINEMENT AT 2.0 ANGSTROMS RESOLUTION. | Descriptor: | BILIN BINDING PROTEIN, BILIVERDIN IX GAMMA CHROMOPHORE | Authors: | Huber, R, Schneider, M, Mayr, I, Mueller, R, Deutzmann, R, Suter, F, Zuber, H, Falk, H, Kayser, H. | Deposit date: | 1990-09-19 | Release date: | 1991-10-15 | Last modified: | 2017-11-29 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution. J.Mol.Biol., 198, 1987
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6XIA
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3SGA
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1FXI
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8ICD
| REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE | Descriptor: | ISOCITRATE DEHYDROGENASE, ISOCITRIC ACID, MAGNESIUM ION | Authors: | Hurley, J.H, Dean, A.M, Sohl, J.L, Koshlandjunior, D.E, Stroud, R.M. | Deposit date: | 1990-05-30 | Release date: | 1991-10-15 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Regulation of an enzyme by phosphorylation at the active site. Science, 249, 1990
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1L44
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1L58
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1L64
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