6WH1
| Structure of the complex of human DNA ligase III-alpha and XRCC1 BRCT domains | 分子名称: | DNA ligase 3 alpha, X-ray repair cross complementing protein 1 variant | 著者 | Pourfarjam, Y, Ellenberger, T, Tainer, J.A, Tomkinson, A.E, Kim, I.K. | 登録日 | 2020-04-07 | 公開日 | 2020-12-02 | 最終更新日 | 2024-03-06 | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | 主引用文献 | An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase III alpha within a flexible DNA repair complex. Nucleic Acids Res., 49, 2021
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6WH2
| Structure of the C-terminal BRCT domain of human XRCC1 | 分子名称: | X-ray repair cross complementing protein 1 variant | 著者 | Pourfarjam, Y, Ellenberger, T, Tainer, J.A, Tomkinson, A.E, Kim, I.K. | 登録日 | 2020-04-07 | 公開日 | 2020-12-02 | 最終更新日 | 2023-10-18 | 実験手法 | X-RAY DIFFRACTION (2.414 Å) | 主引用文献 | An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase III alpha within a flexible DNA repair complex. Nucleic Acids Res., 49, 2021
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6D3A
| Structure of human ARH3 D314E bound to ADP-ribose and magnesium | 分子名称: | MAGNESIUM ION, Poly(ADP-ribose) glycohydrolase ARH3, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE | 著者 | Pourfarjam, Y, Ventura, J, Kurinov, I, Kim, I.K. | 登録日 | 2018-04-15 | 公開日 | 2018-06-20 | 最終更新日 | 2024-03-13 | 実験手法 | X-RAY DIFFRACTION (1.60001016 Å) | 主引用文献 | Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J.Biol.Chem., 293, 2018
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6D36
| Structure of human ARH3 bound to ADP-ribose and magnesium | 分子名称: | MAGNESIUM ION, Poly(ADP-ribose) glycohydrolase ARH3, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE | 著者 | Pourfarjam, Y, Ventura, J, Kurinov, I, Kim, I.K. | 登録日 | 2018-04-14 | 公開日 | 2018-06-20 | 最終更新日 | 2023-10-04 | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | 主引用文献 | Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J.Biol.Chem., 293, 2018
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7L9H
| Crystal structure of human ARH3-D77A bound to magnesium and ADP-ribose | 分子名称: | ADP-ribose glycohydrolase ARH3, MAGNESIUM ION, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE | 著者 | Pourfarjam, Y, Kurinov, I, Moss, J, Kim, I.K. | 登録日 | 2021-01-04 | 公開日 | 2021-04-28 | 最終更新日 | 2023-10-18 | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | 主引用文献 | Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions. J.Biol.Chem., 296, 2021
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7L9I
| Crystal structure of human ARH3-D314A bound to magnesium and ADP-ribose | 分子名称: | ADP-ribose glycohydrolase ARH3, MAGNESIUM ION, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE | 著者 | Pourfarjam, Y, Kurinov, I, Moss, J, Kim, I.K. | 登録日 | 2021-01-04 | 公開日 | 2021-04-28 | 最終更新日 | 2023-10-18 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions. J.Biol.Chem., 296, 2021
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7L9F
| Crystal structure of human ARH3 bound to calcium and ADP-ribose | 分子名称: | CALCIUM ION, Poly(ADP-ribose) glycohydrolase ARH3, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE | 著者 | Pourfarjam, Y, Kurinov, I, Moss, J, Kim, I.K. | 登録日 | 2021-01-04 | 公開日 | 2021-04-28 | 最終更新日 | 2023-10-18 | 実験手法 | X-RAY DIFFRACTION (1.75 Å) | 主引用文献 | Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions. J.Biol.Chem., 296, 2021
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