5ET4
 
 | | Structure of RNase A-K7H/R10H in complex with 3'-CMP | | 分子名称: | (4S)-2-METHYL-2,4-PENTANEDIOL, CYTIDINE-3'-MONOPHOSPHATE, Ribonuclease pancreatic | | 著者 | Blanco, J.A, Salazar, V.A, Moussaoui, M, Boix, E. | | 登録日 | 2015-11-17 | | 公開日 | 2016-11-30 | | 最終更新日 | 2024-01-10 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates.
Biochim Biophys Acta Gen Subj, 1863, 2019
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5OGH
 | | Structure of RNase A at high resolution (1.16 A) in complex with 3'-CMP and sulphate ions | | 分子名称: | CHLORIDE ION, CYTIDINE-3'-MONOPHOSPHATE, Ribonuclease pancreatic, ... | | 著者 | Blanco, J.A, Prats-Ejarque, G, Salazar, V.A, Moussaoui, M, Boix, E. | | 登録日 | 2017-07-13 | | 公開日 | 2018-08-01 | | 最終更新日 | 2024-01-17 | | 実験手法 | X-RAY DIFFRACTION (1.16 Å) | | 主引用文献 | Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates.
Biochim Biophys Acta Gen Subj, 1863, 2019
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6ENP
 | | Atomic resolution structure of human RNase 6 in the presence of phosphate anions in P21 space group. | | 分子名称: | CHLORIDE ION, PHOSPHATE ION, Ribonuclease K6, ... | | 著者 | Prats-Ejarque, G, Moussaoui, M, Boix, E. | | 登録日 | 2017-10-05 | | 公開日 | 2018-10-24 | | 最終更新日 | 2024-01-17 | | 実験手法 | X-RAY DIFFRACTION (1.042 Å) | | 主引用文献 | Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates.
Biochim Biophys Acta Gen Subj, 1863, 2019
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5OAB
 | | A novel crystal form of human RNase6 at atomic resolution | | 分子名称: | CHLORIDE ION, PHOSPHATE ION, POTASSIUM ION, ... | | 著者 | Prats-Ejarque, G, Moussaoui, M, Boix, E. | | 登録日 | 2017-06-21 | | 公開日 | 2018-08-01 | | 最終更新日 | 2024-01-17 | | 実験手法 | X-RAY DIFFRACTION (1.111 Å) | | 主引用文献 | Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates.
Biochim Biophys Acta Gen Subj, 1863, 2019
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