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Yorodumi- EMDB-30965: Cryo-EM map of the conformation 1 of S-ACE2-B0AT1 ternary complex... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-30965 | ||||||||||||
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| Title | Cryo-EM map of the conformation 1 of S-ACE2-B0AT1 ternary complex focused right SARS-CoV-2 | ||||||||||||
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Sample |
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| Function / homology | Function and homology informationsymbiont-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 ...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 | ![]() | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 6.7 Å | ||||||||||||
Authors | Yan RH / Zhang YY | ||||||||||||
| Funding support | China, 3 items
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Citation | Journal: Cell Res / Year: 2021Title: Structural basis for the different states of the spike protein of SARS-CoV-2 in complex with ACE2. Authors: Renhong Yan / Yuanyuan Zhang / Yaning Li / Fangfei Ye / Yingying Guo / Lu Xia / Xinyue Zhong / Ximin Chi / Qiang Zhou / ![]() | ||||||||||||
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_30965.map.gz | 44.6 MB | EMDB map data format | |
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| Header (meta data) | emd-30965-v30.xml emd-30965.xml | 9.1 KB 9.1 KB | Display Display | EMDB header |
| Images | emd_30965.png | 57.1 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-30965 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30965 | HTTPS FTP |
-Validation report
| Summary document | emd_30965_validation.pdf.gz | 313.5 KB | Display | EMDB validaton report |
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| Full document | emd_30965_full_validation.pdf.gz | 313.1 KB | Display | |
| Data in XML | emd_30965_validation.xml.gz | 6.6 KB | Display | |
| Data in CIF | emd_30965_validation.cif.gz | 7.3 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30965 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30965 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7dwxC ![]() 7dwyC ![]() 7dwzC ![]() 7dx0C ![]() 7dx1C ![]() 7dx2C ![]() 7dx3C ![]() 7dx5C ![]() 7dx6C ![]() 7dx7C ![]() 7dx8C ![]() 7dx9C C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_30965.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Cryo-EM map of the conformation 1 of S-ACE2-B0AT1 ternary complex...
| Entire | Name: Cryo-EM map of the conformation 1 of S-ACE2-B0AT1 ternary complex focused right SARS-CoV-2 |
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| Components |
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-Supramolecule #1: Cryo-EM map of the conformation 1 of S-ACE2-B0AT1 ternary complex...
| Supramolecule | Name: Cryo-EM map of the conformation 1 of S-ACE2-B0AT1 ternary complex focused right SARS-CoV-2 type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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| Source (natural) | Organism: ![]() |
| Recombinant expression | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 53141 |
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| Initial angle assignment | Type: ANGULAR RECONSTITUTION |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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About Yorodumi



Authors
China, 3 items
Citation
UCSF Chimera







































Z (Sec.)
Y (Row.)
X (Col.)





















Homo sapiens (human)
