6E34
| Capsid protein of PCV2 with N,O6-DISULFO-GLUCOSAMINE and 2-O-sulfo-alpha-L-idopyranuronic acid | Descriptor: | 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose, Capsid protein of PCV2 | Authors: | Khayat, R, Dhindwal, S. | Deposit date: | 2018-07-13 | Release date: | 2018-12-26 | Last modified: | 2024-03-13 | Method: | ELECTRON MICROSCOPY (3.6 Å) | Cite: | Porcine Circovirus 2 Uses a Multitude of Weak Binding Sites To Interact with Heparan Sulfate, and the Interactions Do Not Follow the Symmetry of the Capsid. J.Virol., 93, 2019
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6E2X
| Mechanism of cellular recognition by PCV2 | Descriptor: | 2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose, Capsid protein of PCV2 | Authors: | Khayat, R, Dhindwal, S. | Deposit date: | 2018-07-12 | Release date: | 2018-12-26 | Last modified: | 2024-03-13 | Method: | ELECTRON MICROSCOPY (3.5 Å) | Cite: | Porcine Circovirus 2 Uses a Multitude of Weak Binding Sites To Interact with Heparan Sulfate, and the Interactions Do Not Follow the Symmetry of the Capsid. J.Virol., 93, 2019
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6E30
| Mechanism of cellular recognition by PCV2 | Descriptor: | 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose, Capsid protein of PCV2 | Authors: | Khayat, R, Dhindwal, S. | Deposit date: | 2018-07-12 | Release date: | 2018-12-26 | Last modified: | 2024-03-13 | Method: | ELECTRON MICROSCOPY (3.5 Å) | Cite: | Porcine Circovirus 2 Uses a Multitude of Weak Binding Sites To Interact with Heparan Sulfate, and the Interactions Do Not Follow the Symmetry of the Capsid. J.Virol., 93, 2019
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6E2Z
| Mechanism of cellular recognition by PCV2 | Descriptor: | 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose, Capsid protein of PCV2 | Authors: | Khayat, R, Dhindwal, S. | Deposit date: | 2018-07-12 | Release date: | 2018-12-26 | Last modified: | 2024-03-13 | Method: | ELECTRON MICROSCOPY (3.4 Å) | Cite: | Porcine Circovirus 2 Uses a Multitude of Weak Binding Sites To Interact with Heparan Sulfate, and the Interactions Do Not Follow the Symmetry of the Capsid. J.Virol., 93, 2019
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3OLF
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3OOF
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3OOK
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3OKI
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3OMM
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3OMK
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3OKH
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6LXT
| Structure of post fusion core of 2019-nCoV S2 subunit | Descriptor: | Spike protein S2, TETRAETHYLENE GLYCOL, ZINC ION | Authors: | Zhu, Y, Sun, F. | Deposit date: | 2020-02-11 | Release date: | 2020-02-26 | Last modified: | 2023-11-29 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. Cell Res., 30, 2020
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4FSX
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4FT4
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4FT2
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5EIB
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6OIT
| CryoEM structure of Arabidopsis DDR' complex (DRD1 peptide-DMS3-RDM1) | Descriptor: | Protein CHROMATIN REMODELING 35, Protein DEFECTIVE IN MERISTEM SILENCING 3, Protein RDM1 | Authors: | Wongpalee, S.P, Liu, S, Zhou, Z.H, Jacobsen, S.E. | Deposit date: | 2019-04-09 | Release date: | 2019-07-24 | Last modified: | 2024-03-20 | Method: | ELECTRON MICROSCOPY (3.5 Å) | Cite: | CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation. Nat Commun, 10, 2019
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6OIS
| CryoEM structure of Arabidopsis DR complex (DMS3-RDM1) | Descriptor: | Protein DEFECTIVE IN MERISTEM SILENCING 3, Protein RDM1 | Authors: | Wongpalee, S.P, Liu, S, Zhou, Z.H, Jacobsen, S.E. | Deposit date: | 2019-04-09 | Release date: | 2019-07-24 | Last modified: | 2024-03-20 | Method: | ELECTRON MICROSCOPY (3.6 Å) | Cite: | CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation. Nat Commun, 10, 2019
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8FC8
| Cryo-EM structure of the human TRPV4 in complex with GSK1016790A | Descriptor: | CHOLESTEROL HEMISUCCINATE, N-[(2S)-1-{4-[N-(2,4-dichlorobenzene-1-sulfonyl)-L-seryl]piperazin-1-yl}-4-methyl-1-oxopentan-2-yl]-1-benzothiophene-2-carboxamide, Transient receptor potential cation channel subfamily V member 4 | Authors: | Kwon, D.H, Lee, S.-Y, Zhang, F. | Deposit date: | 2022-12-01 | Release date: | 2023-07-12 | Method: | ELECTRON MICROSCOPY (3.47 Å) | Cite: | TRPV4-Rho GTPase complex structures reveal mechanisms of gating and disease. Nat Commun, 14, 2023
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8FC9
| Cryo-EM structure of the human TRPV4 - RhoA, apo condition | Descriptor: | GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, Transforming protein RhoA, ... | Authors: | Kwon, D.H, Lee, S.-Y, Zhang, F. | Deposit date: | 2022-12-01 | Release date: | 2023-07-12 | Method: | ELECTRON MICROSCOPY (3.75 Å) | Cite: | TRPV4-Rho GTPase complex structures reveal mechanisms of gating and disease. Nat Commun, 14, 2023
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8FCA
| Cryo-EM structure of the human TRPV4 - RhoA in complex with 4alpha-Phorbol 12,13-didecanoate | Descriptor: | (1aR,1bS,4aS,7aS,7bS,8R,9R,9aS)-9a-(decanoyloxy)-4a,7b-dihydroxy-3-(hydroxymethyl)-1,1,6,8-tetramethyl-5-oxo-1a,1b,4,4a,5,7a,7b,8,9,9a-decahydro-1H-cyclopropa[3,4]benzo[1,2-e]azulen-9-yl decanoate, CHOLESTEROL HEMISUCCINATE, Transient receptor potential cation channel subfamily V member 4 | Authors: | Kwon, D.H, Lee, S.-Y, Zhang, F. | Deposit date: | 2022-12-01 | Release date: | 2023-07-12 | Method: | ELECTRON MICROSCOPY (3.41 Å) | Cite: | TRPV4-Rho GTPase complex structures reveal mechanisms of gating and disease. Nat Commun, 14, 2023
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8FCB
| Cryo-EM structure of the human TRPV4 - RhoA in complex with GSK1016790A | Descriptor: | 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, CHOLESTEROL HEMISUCCINATE, N-[(2S)-1-{4-[N-(2,4-dichlorobenzene-1-sulfonyl)-L-seryl]piperazin-1-yl}-4-methyl-1-oxopentan-2-yl]-1-benzothiophene-2-carboxamide, ... | Authors: | Kwon, D.H, Lee, S.-Y, Zhang, F. | Deposit date: | 2022-12-01 | Release date: | 2023-07-12 | Method: | ELECTRON MICROSCOPY (3.52 Å) | Cite: | TRPV4-Rho GTPase complex structures reveal mechanisms of gating and disease. Nat Commun, 14, 2023
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8FC7
| Cryo-EM structure of the human TRPV4 - RhoA in complex with GSK2798745 | Descriptor: | 1-({(5S,7S)-3-[5-(2-hydroxypropan-2-yl)pyrazin-2-yl]-7-methyl-2-oxo-1-oxa-3-azaspiro[4.5]decan-7-yl}methyl)-1H-benzimidazole-6-carbonitrile, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... | Authors: | Kwon, D.H, Lee, S.-Y, Zhang, F. | Deposit date: | 2022-12-01 | Release date: | 2023-07-12 | Method: | ELECTRON MICROSCOPY (3.3 Å) | Cite: | TRPV4-Rho GTPase complex structures reveal mechanisms of gating and disease. Nat Commun, 14, 2023
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3QQ3
| Crystal structure of swine major histocompatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides | Descriptor: | 9-mer peptide from Neuraminidase, Beta-2-microglobulin, MHC class I antigen | Authors: | Zhang, N, Qi, J, Gao, F, Pan, X, Chen, R, Li, Q, Chen, Z, Li, X, Xia, C, Gao, G.F. | Deposit date: | 2011-02-15 | Release date: | 2011-12-28 | Method: | X-RAY DIFFRACTION (2.59 Å) | Cite: | Crystal structure of swine major histocompatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides. J.Virol., 85, 2011
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3QQ4
| Crystal structure of swine major histocompatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides | Descriptor: | Beta-2-microglobulin, MHC class I antigen, VP35 | Authors: | Zhang, N, Qi, J, Gao, F, Pan, X, Chen, R, Li, Q, Chen, Z, Li, X, Xia, C, Gao, G.F. | Deposit date: | 2011-02-15 | Release date: | 2011-12-28 | Last modified: | 2023-11-01 | Method: | X-RAY DIFFRACTION (2.097 Å) | Cite: | Crystal structure of swine major histocompatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides. J.Virol., 85, 2011
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