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- PDB-7fcp: Crystallographic structure of two neutralizing antibodies in comp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7fcp | ||||||
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Title | Crystallographic structure of two neutralizing antibodies in complex with SARS-CoV-2 spike receptor-binding Domain (RBD) | ||||||
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![]() | ANTIVIRAL PROTEIN / SARS-CoV-2 / RBD / neutralizing antibodies | ||||||
Function / homology | ![]() Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane ...Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / entry receptor-mediated virion attachment to host cell / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / membrane fusion / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / receptor ligand activity / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Zheng, P. / Jin, T. | ||||||
![]() | ![]() Title: Ultrapotent neutralizing antibodies against SARS-CoV-2 with a high degree of mutation resistance. Authors: Zou, J. / Li, L. / Zheng, P. / Liang, W. / Hu, S. / Zhou, S. / Wang, Y. / Zhao, J. / Yuan, D. / Liu, L. / Wu, D. / Xu, M. / Zhang, F. / Zhu, M. / Wu, Z. / Cao, X. / Ni, M. / Ling, X. / Wu, Y. ...Authors: Zou, J. / Li, L. / Zheng, P. / Liang, W. / Hu, S. / Zhou, S. / Wang, Y. / Zhao, J. / Yuan, D. / Liu, L. / Wu, D. / Xu, M. / Zhang, F. / Zhu, M. / Wu, Z. / Cao, X. / Ni, M. / Ling, X. / Wu, Y. / Kuang, Z. / Hu, M. / Li, J. / Li, X. / Guo, X. / Xu, T. / Jiang, H. / Gao, C. / Yu, M. / Liu, J. / Zhong, N. / Zhou, J. / Huang, J.A. / Jin, T. / He, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 237.3 KB | Display | ![]() |
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PDB format | ![]() | 183.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 497.7 KB | Display | ![]() |
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Full document | ![]() | 501.9 KB | Display | |
Data in XML | ![]() | 44.2 KB | Display | |
Data in CIF | ![]() | 64.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7fcqC ![]() 6xdgS ![]() 7jmwS S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Antibody , 4 types, 4 molecules HLBD
#2: Antibody | Mass: 25477.451 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#3: Antibody | Mass: 22858.178 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#4: Antibody | Mass: 24304.221 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#5: Antibody | Mass: 23547.059 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein / Sugars , 2 types, 2 molecules A![](data/chem/img/NAG.gif)
![](data/chem/img/NAG.gif)
#1: Protein | Mass: 30940.680 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: S, 2 / Production host: ![]() |
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#7: Sugar | ChemComp-NAG / |
-Non-polymers , 3 types, 592 molecules ![](data/chem/img/TRS.gif)
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![](data/chem/img/HOH.gif)
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![](data/chem/img/HOH.gif)
#6: Chemical | ChemComp-TRS / | ||
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#8: Chemical | #9: Water | ChemComp-HOH / | |
-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.5 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.05 M HEPES pH 7.0 20%(w/v) PEG3350 1%(w/v) Tryptone |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 8, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97852 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→107.06 Å / Num. obs: 48529 / % possible obs: 100 % / Redundancy: 6.3 % / CC1/2: 0.981 / Rmerge(I) obs: 0.08 / Rrim(I) all: 0.088 / Net I/σ(I): 22.4 |
Reflection shell | Resolution: 2.4→2.44 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.719 / Mean I/σ(I) obs: 2.2 / Num. unique obs: 2422 / CC1/2: 0.751 / Rrim(I) all: 0.795 / % possible all: 99.7 |
-Phasing
Phasing | Method: ![]() | |||||||||
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Phasing MR | Model details: Phaser MODE: MR_AUTO
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6XDG, 7JMW Resolution: 2.4→50 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.91 / SU R Cruickshank DPI: 0.4645 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.465 / ESU R Free: 0.27 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 110.66 Å2 / Biso mean: 40.402 Å2 / Biso min: 18.11 Å2
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Refinement step | Cycle: final / Resolution: 2.4→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.461 Å / Rfactor Rfree error: 0
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