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Open data
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Basic information
| Entry | Database: PDB / ID: 9b0h | ||||||||||||||||||||||||
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| Title | In situ human Hibernating class5 80S ribosome | ||||||||||||||||||||||||
 Components | 
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 Keywords | RIBOSOME / In situ | ||||||||||||||||||||||||
| Function / homology |  Function and homology informationSynthesis of diphthamide-EEF2 / translation at postsynapse / response to folic acid / eukaryotic 80S initiation complex / negative regulation of protein neddylation / response to insecticide / regulation of translation involved in cellular response to UV / oxidized pyrimidine DNA binding / response to TNF agonist / negative regulation of endoplasmic reticulum unfolded protein response ...Synthesis of diphthamide-EEF2 / translation at postsynapse / response to folic acid / eukaryotic 80S initiation complex / negative regulation of protein neddylation / response to insecticide / regulation of translation involved in cellular response to UV / oxidized pyrimidine DNA binding / response to TNF agonist / negative regulation of endoplasmic reticulum unfolded protein response / positive regulation of base-excision repair / axial mesoderm development / negative regulation of formation of translation preinitiation complex / regulation of G1 to G0 transition / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / ribosomal protein import into nucleus / positive regulation of cytoplasmic translation / positive regulation of gastrulation / protein tyrosine kinase inhibitor activity / protein-DNA complex disassembly / IRE1-RACK1-PP2A complex / 90S preribosome assembly / positive regulation of endodeoxyribonuclease activity / nucleolus organization / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / positive regulation of Golgi to plasma membrane protein transport / TNFR1-mediated ceramide production / negative regulation of DNA repair / negative regulation of RNA splicing / GAIT complex / positive regulation of DNA damage response, signal transduction by p53 class mediator / supercoiled DNA binding / TORC2 complex binding / neural crest cell differentiation / G1 to G0 transition / NF-kappaB complex / cysteine-type endopeptidase activator activity involved in apoptotic process / oxidized purine DNA binding / positive regulation of ubiquitin-protein transferase activity / aggresome / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / regulation of establishment of cell polarity / negative regulation of bicellular tight junction assembly / ubiquitin-like protein conjugating enzyme binding / middle ear morphogenesis / negative regulation of phagocytosis / rRNA modification in the nucleus and cytosol / Formation of the ternary complex, and subsequently, the 43S complex / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / laminin receptor activity / negative regulation of ubiquitin protein ligase activity / protein kinase A binding / ion channel inhibitor activity / Ribosomal scanning and start codon recognition / pigmentation / homeostatic process / Translation initiation complex formation / lncRNA binding / positive regulation of mitochondrial depolarization / Uptake and function of diphtheria toxin / macrophage chemotaxis / positive regulation of T cell receptor signaling pathway / negative regulation of Wnt signaling pathway / fibroblast growth factor binding / lung morphogenesis / male meiosis I / monocyte chemotaxis / positive regulation of activated T cell proliferation / positive regulation of natural killer cell proliferation / negative regulation of translational frameshifting / TOR signaling / Protein hydroxylation / BH3 domain binding / SARS-CoV-1 modulates host translation machinery / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / cellular response to ethanol / regulation of cell division / iron-sulfur cluster binding / mTORC1-mediated signalling / Peptide chain elongation / Selenocysteine synthesis / skeletal muscle cell differentiation / Formation of a pool of free 40S subunits / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Eukaryotic Translation Termination / ubiquitin ligase inhibitor activity / positive regulation of GTPase activity / cellular response to actinomycin D / blastocyst development / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / translational elongation / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of signal transduction by p53 class mediator / protein serine/threonine kinase inhibitor activity / Viral mRNA Translation / negative regulation of respiratory burst involved in inflammatory response Similarity search - Function  | ||||||||||||||||||||||||
| Biological species |  Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.59 Å | ||||||||||||||||||||||||
 Authors | Wei, Z. / Yong, X. | ||||||||||||||||||||||||
| Funding support | 1items 
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 Citation |  Journal: To Be PublishedTitle: In situ human Hibernating class5 80S ribosome Authors: Wei, Z. / Yong, X.  | ||||||||||||||||||||||||
| 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 |  9b0h.cif.gz | 5.6 MB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb9b0h.ent.gz | Display |  PDB format | |
| PDBx/mmJSON format |  9b0h.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  9b0h_validation.pdf.gz | 2 MB | Display |  wwPDB validaton report | 
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| Full document |  9b0h_full_validation.pdf.gz | 2.2 MB | Display | |
| Data in XML |  9b0h_validation.xml.gz | 374.5 KB | Display | |
| Data in CIF |  9b0h_validation.cif.gz | 658.8 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/b0/9b0h ftp://data.pdbj.org/pub/pdb/validation_reports/b0/9b0h | HTTPS FTP  | 
-Related structure data
| Related structure data | ![]() 44041MC 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
-RNA chain , 5 types, 5 molecules S2L5L7L8Et    
| #1: RNA chain |   Mass: 602776.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
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| #2: RNA chain |   Mass: 1640222.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
| #3: RNA chain |   Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: GenBank: 23898 | 
| #4: RNA chain |   Mass: 50143.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: GenBank: 1142736641 | 
| #85: RNA chain |   Mass: 24102.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
+60S ribosomal protein  ... , 35 types, 35 molecules LALCLFLGLHLJLMLNLOLPLQLRLSLTLVLXLYLZLaLcLdLeLfLgLhLiLjLkLlLn...                              
-Large ribosomal subunit protein  ... , 6 types, 6 molecules LBLDLELLLbLm     
| #6: Protein |   Mass: 46079.918 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P39023 | 
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| #8: Protein |   Mass: 34008.324 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P46777 | 
| #9: Protein |   Mass: 28378.824 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q02878 | 
| #15: Protein |   Mass: 24190.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P26373 | 
| #30: Protein |   Mass: 13965.825 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P47914 | 
| #41: Protein |   Mass: 6199.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62987 | 
-Ribosomal protein  ... , 2 types, 2 molecules LILW 
| #13: Protein |   Mass: 24439.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q96L21 | 
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| #65: Protein |   Mass: 14476.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: A0A994J4A5 | 
-Protein , 7 types, 7 molecules LUCALsSgSfCDCB      
| #24: Protein |   Mass: 11722.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q7Z4W8 | 
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| #47: Protein |   Mass: 39718.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: Q9UQ80 | 
| #48: Protein |   Mass: 21507.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P05388 | 
| #60: Protein |   Mass: 34669.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P63244 | 
| #63: Protein |   Mass: 7884.286 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62979 | 
| #64: Protein |   Mass: 6257.690 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) | 
| #84: Protein |   Mass: 95232.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human)References: UniProt: P13639, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement  | 
-Small ribosomal subunit protein  ... , 10 types, 10 molecules SDSPSQSMSZSESeSHSOSb         
| #50: Protein |   Mass: 25172.561 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P23396 | 
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| #53: Protein |   Mass: 14092.600 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62841 | 
| #54: Protein |   Mass: 16249.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62249 | 
| #61: Protein |   Mass: 13652.019 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P25398 | 
| #62: Protein |   Mass: 8526.119 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62851 | 
| #66: Protein |   Mass: 29523.674 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62701 | 
| #73: Protein |   Mass: 6539.758 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62861 | 
| #76: Protein |   Mass: 21603.229 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62081 | 
| #81: Protein |   Mass: 15014.187 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62263 | 
| #83: Protein |   Mass: 9348.990 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P42677 | 
-40S ribosomal protein  ... , 20 types, 20 molecules SFSKSSSTSUScSdSISLSXSGSJSYSASBSVSaSCSNSW                   
| #51: Protein |   Mass: 21327.723 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P46782 | 
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| #52: Protein |   Mass: 11773.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P46783 | 
| #55: Protein |   Mass: 17029.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62269 | 
| #56: Protein |   Mass: 15822.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P39019 | 
| #57: Protein |   Mass: 11765.890 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P60866 | 
| #58: Protein |   Mass: 7263.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62857 | 
| #59: Protein |   Mass: 6559.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62273 | 
| #67: Protein |   Mass: 24003.012 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62241 | 
| #68: Protein |   Mass: 17785.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62280 | 
| #69: Protein |   Mass: 15626.392 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62266 | 
| #70: Protein |   Mass: 27471.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62753 | 
| #71: Protein |   Mass: 21649.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P46781 | 
| #72: Protein |   Mass: 15203.022 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62847 | 
| #74: Protein |   Mass: 24774.365 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P08865 | 
| #75: Protein |   Mass: 24888.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P61247 | 
| #77: Protein |   Mass: 9124.389 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P63220 | 
| #78: Protein |   Mass: 11742.908 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62854 | 
| #79: Protein |   Mass: 24587.029 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P15880 | 
| #80: Protein |   Mass: 17128.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62277 | 
| #82: Protein |   Mass: 14734.357 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)   Homo sapiens (human) / References: UniProt: P62244 | 
-Non-polymers , 2 types, 261 molecules 


| #86: Chemical | ChemComp-MG / #87: Chemical | ChemComp-ZN /  | 
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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: In situ human Hibernating class5 80S ribosome / Type: RIBOSOME / Entity ID: #1-#85 / Source: NATURAL | 
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| Source (natural) | Organism:  Homo sapiens (human) | 
| Buffer solution | pH: 7.4 | 
| 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: 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: 2500 nm / Nominal defocus min: 1200 nm | 
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) | 
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.59 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 123628 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints | 
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Homo sapiens (human)
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FIELD EMISSION GUN