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Open data
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Basic information
| Entry | Database: PDB / ID: 11hg | |||||||||
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| Title | Rabbit 80S with eEF2,CCDC124,and LARP1,40S-head-swiveled | |||||||||
Components |
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Keywords | RIBOSOME / Hibernation / In extracto Cryo EM / Rabbit | |||||||||
| Function / homology | Function and homology informationSynthesis of diphthamide-EEF2 / translation at postsynapse / glial cell proliferation / skeletal muscle cell differentiation / response to folic acid / positive regulation of cytoplasmic translation / Uptake and function of diphtheria toxin / lncRNA binding / gastrulation / translational elongation ...Synthesis of diphthamide-EEF2 / translation at postsynapse / glial cell proliferation / skeletal muscle cell differentiation / response to folic acid / positive regulation of cytoplasmic translation / Uptake and function of diphtheria toxin / lncRNA binding / gastrulation / translational elongation / Peptide chain elongation / response to ischemia / ubiquitin ligase inhibitor activity / translation elongation factor activity / positive regulation of signal transduction by p53 class mediator / 90S preribosome / phagocytic cup / skeletal muscle contraction / Protein methylation / cellular response to brain-derived neurotrophic factor stimulus / translation regulator activity / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / positive regulation of apoptotic signaling pathway / MDM2/MDM4 family protein binding / response to endoplasmic reticulum stress / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / positive regulation of translation / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / response to hydrogen peroxide / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / positive regulation of cell differentiation / small-subunit processome / spindle / cytoplasmic ribonucleoprotein granule / p53 binding / rRNA processing / actin filament binding / cytosolic ribosome / azurophil granule lumen / transcription corepressor activity / response to estradiol / regulation of translation / rhythmic process / large ribosomal subunit / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / antimicrobial humoral immune response mediated by antimicrobial peptide / large ribosomal subunit rRNA binding / secretory granule lumen / killing of cells of another organism / defense response to Gram-negative bacterium / ficolin-1-rich granule lumen / cytosolic large ribosomal subunit / nucleic acid binding / response to ethanol / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / perikaryon / cell differentiation / cytoplasmic translation / postsynapse / postsynaptic density / negative regulation of translation / mitochondrial inner membrane / response to xenobiotic stimulus / rRNA binding / cadherin binding / ribosome / translation / structural constituent of ribosome / ribonucleoprotein complex / cell division / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / DNA repair / apoptotic process / mRNA binding / centrosome / GTPase activity / negative regulation of apoptotic process / Neutrophil degranulation / nucleolus / synapse / dendrite / protein kinase binding / GTP binding / perinuclear region of cytoplasm / glutamatergic synapse / endoplasmic reticulum / DNA binding / DNA-templated transcription 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 | 11hg.cif.gz | 5.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb11hg.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 11hg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1h/11hg ftp://data.pdbj.org/pub/pdb/validation_reports/1h/11hg | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 75689MC ![]() 11heC ![]() 11hvC ![]() 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 , 12 types, 12 molecules BBPP42stFAARRUUvLACE
| #1: Protein | Mass: 24361.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: Protein | Mass: 9124.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #41: Protein | Mass: 12198.603 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #47: Protein | Mass: 21521.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #48: Protein | Mass: 16561.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 39962.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 34669.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #63: Protein | Mass: 15844.666 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #76: Protein | Mass: 11645.794 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is GenBank XP_051702317.1 Source: (natural) ![]() |
| #80: Protein | Mass: 95474.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P13639, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
| #81: Protein | Mass: 123705.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #82: Protein | Mass: 25890.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-40S ribosomal protein ... , 20 types, 20 molecules S2ASFFVVZZEETTWWCCOOLLXXSSS6S4S9YYRSWXS8
| #2: Protein | Mass: 24441.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #44: Protein | Mass: 24759.145 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #45: Protein | Mass: 17057.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #46: Protein | Mass: 9348.990 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #51: Protein | Mass: 7986.440 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #52: Protein | Mass: 13048.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #53: Protein | Mass: 8526.119 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: Protein | Mass: 7007.069 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #57: Protein | Mass: 11529.682 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #59: Protein | Mass: 11395.489 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #61: Protein | Mass: 16898.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #62: Protein | Mass: 6559.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #64: Protein | Mass: 14432.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #65: Protein | Mass: 27471.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #66: Protein | Mass: 29523.674 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #67: Protein | Mass: 21649.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #69: Protein | Mass: 6317.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: SLARVGKVRGQTLKVAKQEKKKKRTGRAKRRMQYNRRFVNVVPTFGKKKGPNANS Source: (natural) ![]() |
| #71: Protein | Mass: 15250.714 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #72: Protein | Mass: 14734.357 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #73: Protein | Mass: 24003.012 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is GenBank XP_017201844.1 Source: (natural) ![]() |
-Small ribosomal subunit protein ... , 8 types, 8 molecules DDS5IIMMS7S3GGA
| #4: Protein | Mass: 17586.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #54: Protein | Mass: 21525.941 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #56: Protein | Mass: 16032.804 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #60: Protein | Mass: 15611.003 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is GenBank XP_069928942.1 Source: (natural) ![]() |
| #68: Protein | Mass: 21629.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #70: Protein | Mass: 23704.916 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: G1TNM3, DNA-(apurinic or apyrimidinic site) lyase |
| #75: Protein | Mass: 14544.659 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #83: Protein | Mass: 14065.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RNA chain , 5 types, 5 molecules 58618ES28
| #5: RNA chain | Mass: 50143.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #6: RNA chain | Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: >7TOR_4|Chain D[auth A5S]|5S rRNA|Oryctolagus cuniculus Source: (natural) ![]() |
| #79: RNA chain | Mass: 544906.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #84: RNA chain | Mass: 1640122.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #85: RNA chain | Mass: 1556599.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 25 types, 25 molecules L8L3L4L5L71314151719212627dd30313435363739ffgg11L9
-Large ribosomal subunit protein ... , 12 types, 12 molecules L6aabb2022cc2932ee3840Q
| #11: Protein | Mass: 28818.293 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #13: Protein | Mass: 27351.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is GenBank XP_069914725.1 Source: (natural) ![]() |
| #18: Protein | Mass: 23144.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 20827.561 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: 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 Details: Author-provided sequence reference is GenBank XP_069913375.1 Source: (natural) ![]() |
| #32: Protein | Mass: 12449.612 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is GenBank XP_069913375.1 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) ![]() |
| #50: Protein | Mass: 21699.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Author-provided sequence reference is GenBank XP_069919239.1 Source: (natural) ![]() |
-Ribosomal protein ... , 3 types, 3 molecules 10W23
| #14: Protein | Mass: 24511.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #74: Protein | Mass: 14131.536 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #86: Protein | Mass: 14892.505 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide , 1 types, 1 molecules 41
| #40: Protein/peptide | Mass: 3473.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 2 types, 5 molecules 


| #87: Chemical | ChemComp-ZN / #88: Chemical | ChemComp-GDP / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-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: #1-#5, #7-#79, #81-#83, #6, #86 / 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: 8501 / Symmetry type: POINT | ||||||||||||||||||||||||||||
| Atomic model building |
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| Atomic model building |
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| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 131.24 Å2 | ||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






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