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Yorodumi- PDB-9kt3: Structure of EG.5.1 S trimer with 2 down-RBDs complex with antibo... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9kt3 | ||||||
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| Title | Structure of EG.5.1 S trimer with 2 down-RBDs complex with antibody CYFN1006-2. | ||||||
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Keywords | VIRAL PROTEIN/IMMUNE SYSTEM / antibody / viral protein / VIRAL PROTEIN-IMMUNE SYSTEM complex | ||||||
| Function / homology | Function and homology informationvirion component / symbiont-mediated disruption of host tissue / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / viral translation / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion ...virion component / symbiont-mediated disruption of host tissue / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / viral translation / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell / membrane fusion / Attachment and Entry / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / symbiont-mediated suppression of host innate immune response / receptor ligand activity / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / symbiont entry into host cell / 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 | ![]() Escherichia phage T4 (virus)synthetic construct (others) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.63 Å | ||||||
Authors | Wang, Y.J. / Sun, L. | ||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: Structure of EG.5.1 S trimer with 2 down-RBDs complex with antibody CYFN1006-2. Authors: Wang, Y.J. / Sun, L. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9kt3.cif.gz | 782.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9kt3.ent.gz | 630.2 KB | Display | PDB format |
| PDBx/mmJSON format | 9kt3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9kt3_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9kt3_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 9kt3_validation.xml.gz | 121 KB | Display | |
| Data in CIF | 9kt3_validation.cif.gz | 185.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kt/9kt3 ftp://data.pdbj.org/pub/pdb/validation_reports/kt/9kt3 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 62556MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 143147.594 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Escherichia phage T4 (virus), (gene. exp.) synthetic construct (others)Strain: Omicron/EG.5.1 / Gene: S, 2, wac / Production host: Homo sapiens (human) / References: UniProt: P0DTC2, UniProt: P10104#2: Antibody | Mass: 22673.113 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia phage T4 (virus) / Gene: wac / Production host: Homo sapiens (human)#3: Protein | Mass: 23388.381 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: Homo sapiens (human)Has protein modification | Y | |
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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 |
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Sample preparation
| Component | Name: Structure of EG.5.1 S trimer with 2 down-RBDs complex with antibody CYFN1006-2. Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | |||||||||||||||
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| Source (natural) |
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| Source (recombinant) | Organism: Homo sapiens (human) | |||||||||||||||
| Buffer solution | pH: 8 | |||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.17.1_3660 / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.63 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 28052 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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Homo sapiens (human)
FIELD EMISSION GUN