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Open data
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Basic information
| Entry | Database: PDB / ID: 9b0s | |||||||||||||||||||||
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| Title | In situ human top-top di-ribosome structure (Composite map) | |||||||||||||||||||||
Components |
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Keywords | RIBOSOME / In situ | |||||||||||||||||||||
| Function / homology | Function and homology informationEukaryotic Translation Elongation / Synthesis of diphthamide-EEF2 / translation at postsynapse / endothelial cell differentiation / 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 / negative regulation of endoplasmic reticulum unfolded protein response ...Eukaryotic Translation Elongation / Synthesis of diphthamide-EEF2 / translation at postsynapse / endothelial cell differentiation / 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 / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / axial mesoderm development / negative regulation of formation of translation preinitiation complex / positive regulation of respiratory burst involved in inflammatory response / regulation of G1 to G0 transition / ribosomal protein import into nucleus / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / positive regulation of cytoplasmic translation / protein tyrosine kinase inhibitor activity / protein-DNA complex disassembly / positive regulation of endodeoxyribonuclease activity / IRE1-RACK1-PP2A complex / nucleolus organization / positive regulation of Golgi to plasma membrane protein transport / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / 90S preribosome assembly / 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 / aggresome / positive regulation of ubiquitin-protein transferase activity / 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 / positive regulation of DNA binding / 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 / homeostatic process / Translation initiation complex formation / pigmentation / 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 / monocyte chemotaxis / male meiosis I / positive regulation of natural killer cell proliferation / positive regulation of activated T cell proliferation / negative regulation of translational frameshifting / TOR signaling / Protein hydroxylation / BH3 domain binding / SARS-CoV-1 modulates host translation machinery / TFIID-class transcription factor complex binding / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / iron-sulfur cluster binding / regulation of cell division / cellular response to ethanol / mTORC1-mediated signalling / Peptide chain elongation / regulation of lipid metabolic process / Selenocysteine synthesis / Formation of a pool of free 40S subunits / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / skeletal muscle cell differentiation / 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 / Response of EIF2AK4 (GCN2) to amino acid deficiency / blastocyst development / SRP-dependent cotranslational protein targeting to membrane / translational elongation Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||||||||||||||
Authors | Wei, Z. / Yong, X. | |||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: In situ human top-back di-ribosome structure Authors: Wei, Z. / Yong, X. | |||||||||||||||||||||
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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 | 9b0s.cif.gz | 11.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9b0s.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9b0s.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9b0s_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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| Full document | 9b0s_full_validation.pdf.gz | 2 MB | Display | |
| Data in XML | 9b0s_validation.xml.gz | 696.4 KB | Display | |
| Data in CIF | 9b0s_validation.cif.gz | 1.2 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b0/9b0s ftp://data.pdbj.org/pub/pdb/validation_reports/b0/9b0s | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 44052MC 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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Assembly
| Deposited unit | ![]()
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Components
-Protein , 7 types, 11 molecules cHlULUsgSgsfSfcBlsLsCF
| #1: Protein | Mass: 13780.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60869 | ||||||||||
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| #41: Protein | Mass: 11722.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q7Z4W8#75: Protein | Mass: 34669.113 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P63244#78: Protein | Mass: 7884.286 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62979#80: Protein | | Mass: 94322.859 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 #83: Protein | Mass: 21507.035 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P05388#88: Protein | | Mass: 48247.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q5VTE0 |
-Small ribosomal subunit protein ... , 10 types, 20 molecules sESEseSesHSHsOSOsbSbsDSDsPSPsQSQsMSMsZSZ
| #2: Protein | Mass: 29523.674 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62701#9: Protein | Mass: 6539.758 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62861#12: Protein | Mass: 21603.229 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62081#17: Protein | Mass: 15014.187 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62263#19: Protein | Mass: 9348.990 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P42677#65: Protein | Mass: 25172.561 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P23396#68: Protein | Mass: 14092.600 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62841#69: Protein | Mass: 16249.062 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62249#76: Protein | Mass: 13652.019 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P25398#77: Protein | Mass: 8526.119 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62851 |
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+40S ribosomal protein ... , 21 types, 42 molecules sISIsLSLsXSXsGSGsJSJsYSYsASAsBSBsVSVsaSasCSCsNSNsWSWsRSRsFSF...
-RNA chain , 8 types, 13 molecules l7L7l8L8s2S2aPpEEtl5L5ATPt
| #20: RNA chain | Mass: 38691.914 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 23898#21: RNA chain | Mass: 50143.648 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1142736641#79: RNA chain | Mass: 561332.438 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)#81: RNA chain | | Mass: 22885.635 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)#82: RNA chain | Mass: 24102.275 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)#85: RNA chain | Mass: 1211748.500 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)#87: RNA chain | | Mass: 24765.760 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)#89: RNA chain | | Mass: 23825.205 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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+60S ribosomal protein ... , 35 types, 70 molecules lALAlCLClFLFlGLGlHLHlJLJlMLMlNLNlOLOlPLPlQLQlRLRlSLSlTLTlVLV...
-Large ribosomal subunit protein ... , 6 types, 12 molecules lBLBlDLDlELElLLLlbLblmLm
| #23: Protein | Mass: 46079.918 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P39023#25: Protein | Mass: 34008.324 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P46777#26: Protein | Mass: 28378.824 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q02878#32: Protein | Mass: 24190.484 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P26373#47: Protein | Mass: 13965.825 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P47914#58: Protein | Mass: 6199.574 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62987 |
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-Ribosomal protein ... , 2 types, 3 molecules lILILW
| #30: Protein | Mass: 24439.754 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96L21#86: Protein | | Mass: 14476.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: A0A994J4A5 |
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-Non-polymers , 2 types, 522 molecules 


| #90: Chemical | ChemComp-ZN / #91: Chemical | ChemComp-MG / |
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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 top-top di-ribosome / Type: RIBOSOME / Entity ID: #1-#89 / 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: 2000 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: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 9137 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation




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FIELD EMISSION GUN