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Open data
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Basic information
| Entry | Database: PDB / ID: 11hv | |||||||||
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| Title | Rabbit 60S ribosomal subunit with eEF2 domain IV open | |||||||||
Components |
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Keywords | RIBOSOME / Hibernation / In extracto Cryo EM / Rabbit | |||||||||
| Function / homology | Function and homology informationubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / rough endoplasmic reticulum / MDM2/MDM4 family protein binding / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / positive regulation of cell differentiation / cytoplasmic ribonucleoprotein granule / rRNA processing / azurophil granule lumen ...ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / rough endoplasmic reticulum / MDM2/MDM4 family protein binding / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / positive regulation of cell differentiation / cytoplasmic ribonucleoprotein granule / rRNA processing / azurophil granule lumen / transcription corepressor activity / regulation of translation / large ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit rRNA binding / killing of cells of another organism / defense response to Gram-negative bacterium / cytosolic large ribosomal subunit / nucleic acid binding / cytoplasmic translation / tRNA binding / postsynaptic density / negative regulation of translation / rRNA binding / ribosome / translation / structural constituent of ribosome / ribonucleoprotein complex / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / mRNA binding / negative regulation of apoptotic process / Neutrophil degranulation / nucleolus / synapse / endoplasmic reticulum / DNA-templated transcription / RNA binding / extracellular exosome / extracellular region / zinc ion binding / membrane / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Seraj, Z. / Zottig, X. / Huang, C.H. / Loveland, A.B. / Diggs, S. / Sholi, E. / Grigorieff, N. / Korostelev, A.A. | |||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: In extracto cryo-EM reveals eEF2 as a major hibernation factor on 60S and 80S particles Authors: Seraj, Z. / Zottig, X. / Huang, C.H. / Loveland, A.B. / Diggs, S. / Sholi, E. / Grigorieff, N. / Korostelev, A.A. | |||||||||
| History |
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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 | 11hv.cif.gz | 3.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb11hv.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 11hv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1h/11hv ftp://data.pdbj.org/pub/pdb/validation_reports/1h/11hv | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 75704MC ![]() 11heC ![]() 11hgC ![]() 11iqC ![]() 11jjC ![]() 11khC 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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| 1 |
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Components
-Protein , 5 types, 5 molecules v42stEB
| #1: Protein | Mass: 95463.211 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #40: Protein | Mass: 12198.603 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 21521.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 16561.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #45: Protein | Mass: 41869.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RNA chain , 4 types, 4 molecules 585ES28
| #2: RNA chain | Mass: 50143.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: RNA chain | Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #48: RNA chain | Mass: 1640122.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: RNA chain | Mass: 1556278.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 25 types, 25 molecules L8L3L4L5L7L91114151719212627dd30313435363739ffggu
-Large ribosomal subunit protein ... , 14 types, 14 molecules L6aa13bb2022cc2932ee3840Q25
| #8: Protein | Mass: 28818.293 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #10: Protein | Mass: 30089.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is GenBank XP_069914725.1 Source: (natural) ![]() |
| #14: Protein | Mass: 30121.537 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is XP_051696694.1 Source: (natural) ![]() |
| #17: Protein | Mass: 23144.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 20827.561 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: reference is : 7TOR_23|Chain W[auth AL20]|eL20|Oryctolagus cuniculus EM map also support this model. Source: (natural) ![]() |
| #22: Protein | Mass: 11495.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #24: Protein | Mass: 13727.181 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #28: Protein | Mass: 26708.707 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #31: Protein | Mass: 15022.021 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #32: Protein | Mass: 12449.612 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: Protein | Mass: 8107.752 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #39: Protein | Mass: 6199.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #47: Protein | Mass: 21568.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #50: Protein | Mass: 14761.307 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Ribosomal protein ... , 2 types, 2 molecules 1024
| #12: Protein | Mass: 24511.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #23: Protein | Mass: 7512.774 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 4 molecules 


| #51: Chemical | ChemComp-GDP / |
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| #52: Chemical |
-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: CELL / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Rabbit Reticulocyte Lysate / Type: RIBOSOME / Entity ID: #2-#22, #50, #23-#49 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.3 |
| 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: OTHER / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: OTHER / Nominal defocus max: 2000 nm / Nominal defocus min: 700 nm |
| Image recording | Electron dose: 39 e/Å2 / Film or detector model: OTHER |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| 3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 15960 / Symmetry type: POINT |
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