6H2Y
| human Fab 1E6 bound to fHbp variant 3 from Neisseria meningitidis serogroup B | 分子名称: | 1,2-ETHANEDIOL, 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, DI(HYDROXYETHYL)ETHER, ... | 著者 | Veggi, D, Bianchi, F, Cozzi, R, Malito, E, Bottomley, M.J. | 登録日 | 2018-07-17 | 公開日 | 2019-08-14 | 最終更新日 | 2020-02-26 | 実験手法 | X-RAY DIFFRACTION (2.65 Å) | 主引用文献 | Cocrystal structure of meningococcal factor H binding protein variant 3 reveals a new crossprotective epitope recognized by human mAb 1E6. Faseb J., 33, 2019
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5LJM
| Structure of SPATA2 PUB domain | 分子名称: | GLYCEROL, Spermatogenesis-associated protein 2 | 著者 | Elliott, P.R, Komander, D. | 登録日 | 2016-07-18 | 公開日 | 2016-08-24 | 最終更新日 | 2024-05-01 | 実験手法 | X-RAY DIFFRACTION (1.454 Å) | 主引用文献 | SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC Signaling. Mol.Cell, 63, 2016
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3JSX
| X-ray Crystal structure of NAD(P)H: Quinone Oxidoreductase-1 (NQO1) bound to the coumarin-based inhibitor AS1 | 分子名称: | 4-hydroxy-6,7-dimethyl-3-(naphthalen-1-ylmethyl)-2H-chromen-2-one, FLAVIN-ADENINE DINUCLEOTIDE, NAD(P)H dehydrogenase [quinone] 1 | 著者 | Dunstan, M.S, Levy, C, Leys, D. | 登録日 | 2009-09-11 | 公開日 | 2010-01-12 | 最終更新日 | 2023-11-01 | 実験手法 | X-RAY DIFFRACTION (2.45 Å) | 主引用文献 | Synthesis and biological evaluation of coumarin-based inhibitors of NAD(P)H: quinone oxidoreductase-1 (NQO1). J.Med.Chem., 52, 2009
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1VL9
| Atomic resolution (0.97A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 | 分子名称: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, ... | 著者 | Sekar, K, Velmurugan, D, Rajakannan, V, Gayathri, D, Poi, M.-J, Tsai, M.-D, Dauter, M, Dauter, Z. | 登録日 | 2004-07-15 | 公開日 | 2004-10-19 | 最終更新日 | 2023-12-27 | 実験手法 | X-RAY DIFFRACTION (0.97 Å) | 主引用文献 | Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2. Acta Crystallogr.,Sect.F, 61, 2005
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5LPJ
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6XLE
| Full-length Hsc82 in complex with two Aha1 CTD in the presence of AMP-PNP | 分子名称: | ATP-dependent molecular chaperone HSC82, Hsp90 co-chaperone AHA1, MAGNESIUM ION, ... | 著者 | Liu, Y.X, Sun, M, Myasnikov, A.G, Elnatan, D, Agard, D.A. | 登録日 | 2020-06-28 | 公開日 | 2021-06-30 | 最終更新日 | 2024-03-06 | 実験手法 | ELECTRON MICROSCOPY (2.74 Å) | 主引用文献 | Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1 To Be Published
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6XLB
| Apo full-length Hsc82 in complex with Aha1 | 分子名称: | ATP-dependent molecular chaperone HSC82, Hsp90 co-chaperone AHA1 | 著者 | Liu, Y.X, Sun, M, Myasnikov, A.G, Elnatan, D, Agard, D.A. | 登録日 | 2020-06-28 | 公開日 | 2021-06-30 | 最終更新日 | 2024-03-06 | 実験手法 | ELECTRON MICROSCOPY (3.8 Å) | 主引用文献 | Apo full-length Hsc82 in complex with Aha1 To Be Published
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6XLG
| Full-length Hsc82 in complex with two Aha1 CTD in the presence of ATPgammaS | 分子名称: | ATP-dependent molecular chaperone HSC82, Hsp90 co-chaperone AHA1, MAGNESIUM ION, ... | 著者 | Liu, Y.X, Sun, M, Myasnikov, A.G, Elnatan, D, Agard, D.A. | 登録日 | 2020-06-28 | 公開日 | 2021-06-30 | 最終更新日 | 2024-03-06 | 実験手法 | ELECTRON MICROSCOPY (2.71 Å) | 主引用文献 | Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1 To Be Published
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6XLF
| Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP | 分子名称: | ATP-dependent molecular chaperone HSC82, Hsp90 co-chaperone AHA1, MAGNESIUM ION, ... | 著者 | Liu, Y.X, Sun, M, Myasnikov, A.G, Elnatan, D, Agard, D.A. | 登録日 | 2020-06-28 | 公開日 | 2021-06-30 | 実験手法 | ELECTRON MICROSCOPY (3.15 Å) | 主引用文献 | Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1 To Be Published
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6XLH
| Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS | 分子名称: | ADENOSINE-5'-DIPHOSPHATE, ATP-dependent molecular chaperone HSC82, Hsp90 co-chaperone AHA1, ... | 著者 | Liu, Y.X, Sun, M, Myasnikov, A.G, Elnatan, D, Agard, D.A. | 登録日 | 2020-06-28 | 公開日 | 2021-06-30 | 最終更新日 | 2024-03-06 | 実験手法 | ELECTRON MICROSCOPY (2.83 Å) | 主引用文献 | Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1 To Be Published
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5LTL
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6RPH
| TR-SMX open state structure (10-15ms) of bacteriorhodopsin | 分子名称: | Bacteriorhodopsin, RETINAL | 著者 | Weinert, T, Skopintsev, P, James, D, Kekilli, D, Furrer, A, Bruenle, S, Mous, S, Nogly, P, Standfuss, J. | 登録日 | 2019-05-14 | 公開日 | 2019-07-17 | 最終更新日 | 2019-07-24 | 実験手法 | X-RAY DIFFRACTION (2.6 Å) | 主引用文献 | Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science, 365, 2019
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6XLD
| Full-length Hsc82 in complex with Aha1 CTD in the presence of AMPPNP | 分子名称: | ATP-dependent molecular chaperone HSC82, Hsp90 co-chaperone AHA1, MAGNESIUM ION, ... | 著者 | Liu, Y.X, Sun, M, Myasnikov, A.G, Elnatan, D, Agard, D.A. | 登録日 | 2020-06-28 | 公開日 | 2021-06-30 | 最終更新日 | 2024-03-06 | 実験手法 | ELECTRON MICROSCOPY (3.66 Å) | 主引用文献 | Full-length Hsc82 in complex with Aha1 CTD in the presence of AMPPNP To Be Published
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1H6B
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1GZN
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6UOE
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7XRP
| Cryo-EM structure of SARS-CoV-2 spike protein in complex with nanobody C5G2 (localized refinement) | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose, C5G2 nanobody, Spike protein S1 | 著者 | Liu, L, Sun, H, Jiang, Y, Liu, X, Zhao, D, Zheng, Q, Li, S, Xia, N. | 登録日 | 2022-05-11 | 公開日 | 2022-10-05 | 実験手法 | ELECTRON MICROSCOPY (3.88 Å) | 主引用文献 | A potent synthetic nanobody with broad-spectrum activity neutralizes SARS-CoV-2 virus and the Omicron variant BA.1 through a unique binding mode. J Nanobiotechnology, 20, 2022
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7UEL
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7UEM
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7USB
| CCoV-HuPn-2018 S in the swung out conformation (local refinement of domain 0) | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Spike glycoprotein | 著者 | Tortorici, M.A, Veesler, D, Seattle Structural Genomics Center for Infectious Disease (SSGCID) | 登録日 | 2022-04-23 | 公開日 | 2022-08-24 | 実験手法 | ELECTRON MICROSCOPY (3.1 Å) | 主引用文献 | Structure, receptor recognition, and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein. Cell, 185, 2022
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7UEN
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7US9
| CCoV-HuPn-2018 S in the proximal conformation (local refinement of domain 0) | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Spike glycoprotein | 著者 | Tortorici, M.A, Veesler, D, Seattle Structural Genomics Center for Infectious Disease (SSGCID) | 登録日 | 2022-04-23 | 公開日 | 2022-08-24 | 実験手法 | ELECTRON MICROSCOPY (3.8 Å) | 主引用文献 | Structure, receptor recognition, and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein. Cell, 185, 2022
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7AAP
| Nsp7-Nsp8-Nsp12 SARS-CoV2 RNA-dependent RNA polymerase in complex with template:primer dsRNA and favipiravir-RTP | 分子名称: | MAGNESIUM ION, Non-structural protein 12, Non-structural protein 7, ... | 著者 | Naydenova, K, Muir, K.W, Wu, L.F, Zhang, Z, Coscia, F, Peet, M, Castro-Hartman, P, Qian, P, Sader, K, Dent, K, Kimanius, D, Sutherland, J.D, Lowe, J, Barford, D, Russo, C.J. | 登録日 | 2020-09-04 | 公開日 | 2020-09-23 | 最終更新日 | 2024-07-10 | 実験手法 | ELECTRON MICROSCOPY (2.5 Å) | 主引用文献 | Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP. Proc.Natl.Acad.Sci.USA, 118, 2021
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8RKH
| Crystal structure of the ZP-N2 and ZP-N3 domains of mouse ZP2 (mZP2-N2N3) | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Zona pellucida sperm-binding protein 2, ... | 著者 | Fahrenkamp, D, de Sanctis, D, Jovine, L. | 登録日 | 2023-12-25 | 公開日 | 2024-03-13 | 最終更新日 | 2024-03-27 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | ZP2 cleavage blocks polyspermy by modulating the architecture of the egg coat. Cell, 187, 2024
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8RKI
| Molecular basis of ZP3/ZP1 heteropolymerization: crystal structure of a native vertebrate egg coat filament fragment | 分子名称: | Choriogenin H, YTTERBIUM (III) ION, Zona pellucida sperm-binding protein 3, ... | 著者 | Wiseman, B, Zamora-Caballero, S, de Sanctis, D, Yasumasu, S, Jovine, L. | 登録日 | 2023-12-25 | 公開日 | 2024-03-13 | 最終更新日 | 2024-03-27 | 実験手法 | X-RAY DIFFRACTION (4.2 Å) | 主引用文献 | ZP2 cleavage blocks polyspermy by modulating the architecture of the egg coat. Cell, 187, 2024
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