1EQR
| CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI | Descriptor: | ASPARTYL-TRNA SYNTHETASE, MAGNESIUM ION | Authors: | Rees, B, Webster, G, Delarue, M, Boeglin, M, Moras, D. | Deposit date: | 2000-04-06 | Release date: | 2000-06-29 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.7 Å) | Cite: | Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates. J.Mol.Biol., 299, 2000
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1ASY
| CLASS II AMINOACYL TRANSFER RNA SYNTHETASES: CRYSTAL STRUCTURE OF YEAST ASPARTYL-TRNA SYNTHETASE COMPLEXED WITH TRNA ASP | Descriptor: | ASPARTYL-tRNA SYNTHETASE, T-RNA (75-MER) | Authors: | Ruff, M, Cavarelli, J, Rees, B, Krishnaswamy, S, Thierry, J.C, Moras, D. | Deposit date: | 1995-01-19 | Release date: | 1995-05-08 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science, 252, 1991
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1ASZ
| THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION | Descriptor: | ADENOSINE-5'-TRIPHOSPHATE, ASPARTYL-tRNA SYNTHETASE, T-RNA (75-MER) | Authors: | Cavarelli, J, Rees, B, Thierry, J.C, Moras, D. | Deposit date: | 1995-01-19 | Release date: | 1995-05-08 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (3 Å) | Cite: | The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J., 13, 1994
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1EOV
| FREE ASPARTYL-TRNA SYNTHETASE (ASPRS) (E.C. 6.1.1.12) FROM YEAST | Descriptor: | ASPARTYL-TRNA SYNTHETASE | Authors: | Sauter, C, Lorber, B, Cavarelli, J, Moras, D, Giege, R. | Deposit date: | 2000-03-24 | Release date: | 2000-09-24 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J.Mol.Biol., 299, 2000
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