+Open data
-Basic information
Entry | Database: PDB / ID: 8hrj | ||||||
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Title | SARS-CoV-2 Delta variant spike protein | ||||||
Components | Spike glycoprotein | ||||||
Keywords | VIRAL PROTEIN / SARS-CoV-2 / Delta / Spike protein | ||||||
Function / homology | Function and homology information 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 / entry receptor-mediated virion attachment to host cell ...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 / entry receptor-mediated virion attachment to host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / membrane fusion / symbiont-mediated suppression of host innate immune response / 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 | Severe acute respiratory syndrome coronavirus 2 | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||
Authors | Xu, J. / Cheng, H. / Liu, N. / Wang, H.W. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Self-assembled monolayers guided free-standing atomic-crystal/molecule superstructure Authors: Zheng, L. / Xu, J. / Wang, W. / Gao, X. / Liu, N. / Wang, H.W. / Peng, H.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8hrj.cif.gz | 616.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8hrj.ent.gz | 495.1 KB | Display | PDB format |
PDBx/mmJSON format | 8hrj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hr/8hrj ftp://data.pdbj.org/pub/pdb/validation_reports/hr/8hrj | HTTPS FTP |
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-Related structure data
Related structure data | 34975MC 8hriC 8hrkC 8hrlC 8hrmC 8hrnC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 138842.375 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: For the issue of poor atom inclusion, the depositor stated 'we have tried our best to fit the coordinates in the density map of spike via rigid-body dock. However, the flexibility of RBD ...Details: For the issue of poor atom inclusion, the depositor stated 'we have tried our best to fit the coordinates in the density map of spike via rigid-body dock. However, the flexibility of RBD makes it hard to fit, which seems to be general for spike proteins.' Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2 Gene: S, 2 / Production host: Homo sapiens (human) / References: UniProt: P0DTC2 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: SARS-CoV-2 Delta variant spike protein / Type: COMPLEX / Details: on graphene/SAMs membranes / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Severe acute respiratory syndrome coronavirus 2 |
Source (recombinant) | Organism: Homo sapiens (human) |
Buffer solution | pH: 7.8 |
Specimen | Conc.: 0.25 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 1200 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
CTF correction | Type: NONE | ||||||||||||||||||||||||
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3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 75650 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Highest resolution: 3.1 Å | ||||||||||||||||||||||||
Refine LS restraints |
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