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Open data
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Basic information
Entry | Database: PDB / ID: 9b0q | |||||||||||||||||||||
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Title | In situ human top-back di-ribosome structure (Composite map) | |||||||||||||||||||||
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![]() | RIBOSOME / In situ | |||||||||||||||||||||
Function / homology | ![]() Synthesis of diphthamide-EEF2 / endothelial cell differentiation / eukaryotic 80S initiation complex / negative regulation of protein neddylation / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / negative regulation of formation of translation preinitiation complex / regulation of G1 to G0 transition ...Synthesis of diphthamide-EEF2 / endothelial cell differentiation / eukaryotic 80S initiation complex / negative regulation of protein neddylation / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / negative regulation of formation of translation preinitiation complex / regulation of G1 to G0 transition / axial mesoderm development / negative regulation of peptidyl-serine phosphorylation / positive regulation of respiratory burst involved in inflammatory response / ribosomal protein import into nucleus / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / regulation of translation involved in cellular response to UV / positive regulation of gastrulation / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / protein-DNA complex disassembly / protein tyrosine kinase inhibitor activity / 90S preribosome assembly / IRE1-RACK1-PP2A complex / positive regulation of endodeoxyribonuclease activity / nucleolus organization / positive regulation of Golgi to plasma membrane protein transport / translation at postsynapse / TNFR1-mediated ceramide production / negative regulation of DNA repair / negative regulation of RNA splicing / mammalian oogenesis stage / GAIT complex / A band / positive regulation of DNA damage response, signal transduction by p53 class mediator / supercoiled DNA binding / activation-induced cell death of T cells / TORC2 complex binding / neural crest cell differentiation / G1 to G0 transition / NF-kappaB complex / oxidized purine DNA binding / cysteine-type endopeptidase activator activity involved in apoptotic process / aggresome / middle ear morphogenesis / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / translation at presynapse / positive regulation of ubiquitin-protein transferase activity / Formation of the ternary complex, and subsequently, the 43S complex / negative regulation of phagocytosis / erythrocyte homeostasis / rRNA modification in the nucleus and cytosol / positive regulation of DNA binding / cytoplasmic side of rough endoplasmic reticulum membrane / laminin receptor activity / protein kinase A binding / negative regulation of ubiquitin protein ligase activity / pigmentation / Ribosomal scanning and start codon recognition / ion channel inhibitor activity / lncRNA binding / homeostatic process / Translation initiation complex formation / response to aldosterone / positive regulation of mitochondrial depolarization / Uptake and function of diphtheria toxin / positive regulation of T cell receptor signaling pathway / macrophage chemotaxis / positive regulation of activated T cell proliferation / fibroblast growth factor binding / negative regulation of Wnt signaling pathway / lung morphogenesis / male meiosis I / monocyte chemotaxis / negative regulation of translational frameshifting / Protein hydroxylation / BH3 domain binding / TOR signaling / SARS-CoV-1 modulates host translation machinery / TFIID-class transcription factor complex binding / regulation of cell division / mTORC1-mediated signalling / T cell proliferation involved in immune response / Peptide chain elongation / iron-sulfur cluster binding / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / regulation of lipid metabolic process / Selenocysteine synthesis / positive regulation of signal transduction by p53 class mediator / Formation of a pool of free 40S subunits / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ubiquitin ligase inhibitor activity / Eukaryotic Translation Termination / translational elongation / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / blastocyst development / cellular response to actinomycin D / negative regulation of ubiquitin-dependent protein catabolic process Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||||||||||||||
![]() | Wei, Z. / Yong, Z. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: In situ human top-top di-ribosome structure (Composite map) Authors: Wei, Z. / Yong, X. | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 9.9 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 44050MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Protein , 6 types, 12 molecules CHcHlULUsgSgsfSfcBCBlsLs
#1: Protein | Mass: 13780.738 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #41: Protein | Mass: 11722.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #75: Protein | Mass: 34669.113 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #78: Protein | Mass: 7884.286 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #80: Protein | Mass: 95232.875 Da / Num. of mol.: 2 / 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 #83: Protein | Mass: 21507.035 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Small ribosomal subunit protein ... , 11 types, 20 molecules sESEsesHSHsOSOsbSbsDSDsPSPsQSQsMSMsZSZSe
#2: Protein | Mass: 29523.674 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | | Mass: 6539.758 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 21603.229 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 15014.187 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 9348.990 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #65: Protein | Mass: 25172.561 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #68: Protein | Mass: 14092.600 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #69: Protein | Mass: 16249.062 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #76: Protein | Mass: 13652.019 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #77: Protein | Mass: 8526.119 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #86: Protein/peptide | | Mass: 5407.466 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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+40S ribosomal protein ... , 21 types, 42 molecules sISIsLSLsXSXsGSGsJSJsYSYsASAsBSBsVSVsaSasCSCsNSNsWSWsRSRsFSF...
-RNA chain , 6 types, 12 molecules l7L7l8L8s2S2aPAPpEPEl5L5
#20: RNA chain | Mass: 38691.914 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #21: RNA chain | Mass: 50143.648 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #79: RNA chain | Mass: 561332.438 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #81: RNA chain | Mass: 23277.824 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #82: RNA chain | Mass: 24298.369 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #85: RNA chain | Mass: 1211748.500 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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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) ![]() #25: Protein | Mass: 34008.324 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #26: Protein | Mass: 28378.824 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #32: Protein | Mass: 24190.484 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #47: Protein | Mass: 13965.825 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #58: Protein | Mass: 6199.574 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Ribosomal protein ... , 2 types, 4 molecules lILIlWLW
#30: Protein | Mass: 24439.754 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #87: Protein | Mass: 14476.975 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 2 types, 522 molecules 


#88: Chemical | ChemComp-ZN / #89: 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-back di-ribosome / Type: RIBOSOME / Entity ID: #1-#87 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
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: ![]() |
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: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 45867 / Symmetry type: POINT | ||||||||||||||||||||||||
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