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Yorodumi- PDB-9gj5: Human 80S ribosome in complex with NatA in distal position and Ebp1 -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9gj5 | ||||||||||||||||||||||||
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| Title | Human 80S ribosome in complex with NatA in distal position and Ebp1 | ||||||||||||||||||||||||
Components |
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Keywords | TRANSLATION / human 80S ribosome / N-terminal acetylation (NTA) / N-acety-transferase A (NatA) / Ebp1 / PA2G4 | ||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / protein-N-terminal-glutamate acetyltransferase activity / N-terminal amino-acid Nalpha-acetyltransferase NatA / N-terminal protein amino acid acetylation / NatA complex / protein N-terminal-serine acetyltransferase activity / protein-N-terminal-alanine acetyltransferase activity / protein-N-terminal amino-acid acetyltransferase activity / internal protein amino acid acetylation / N-acetyltransferase activity ...negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / protein-N-terminal-glutamate acetyltransferase activity / N-terminal amino-acid Nalpha-acetyltransferase NatA / N-terminal protein amino acid acetylation / NatA complex / protein N-terminal-serine acetyltransferase activity / protein-N-terminal-alanine acetyltransferase activity / protein-N-terminal amino-acid acetyltransferase activity / internal protein amino acid acetylation / N-acetyltransferase activity / acetyltransferase activator activity / eukaryotic 80S initiation complex / regulation of translation involved in cellular response to UV / axial mesoderm development / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / 90S preribosome assembly / positive regulation of DNA damage response, signal transduction by p53 class mediator / TORC2 complex binding / protein acetylation / middle ear morphogenesis / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / chromosome organization / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / protein-RNA complex assembly / rough endoplasmic reticulum / cytosolic ribosome / ossification / positive regulation of translation / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / skeletal system development / positive regulation of cell differentiation / DNA damage response, signal transduction by p53 class mediator / sensory perception of sound / cellular response to gamma radiation / mRNA 5'-UTR binding / Regulation of expression of SLITs and ROBOs / cytoplasmic ribonucleoprotein granule / rRNA processing / azurophil granule lumen / cellular response to UV / transcription corepressor activity / regulation of translation / ribosome binding / cell body / angiogenesis / transcription regulator complex / cytosolic large ribosomal subunit / nucleic acid binding / cytoplasmic translation / cell differentiation / rRNA binding / postsynaptic density / protein stabilization / nuclear body / structural constituent of ribosome / cadherin binding / translation / ribonucleoprotein complex / intracellular membrane-bounded organelle / focal adhesion / negative regulation of DNA-templated transcription / mRNA binding / ubiquitin protein ligase binding / Neutrophil degranulation / synapse / dendrite / regulation of DNA-templated transcription / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / nucleolus / endoplasmic reticulum / DNA binding / RNA binding / extracellular exosome / extracellular region / nucleoplasm / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.61 Å | ||||||||||||||||||||||||
Authors | Klein, M.A. / Wild, K. / Sinning, I. | ||||||||||||||||||||||||
| Funding support | Germany, 1items
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Citation | Journal: To Be PublishedTitle: structure of human RAF complexes Authors: Klein, M.A. / Wild, K. / Sinning, I. | ||||||||||||||||||||||||
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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 | 9gj5.cif.gz | 753.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9gj5.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9gj5.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gj/9gj5 ftp://data.pdbj.org/pub/pdb/validation_reports/gj/9gj5 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 51382MC ![]() 9gj6C 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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Components
-N-alpha-acetyltransferase ... , 2 types, 2 molecules 2B
| #1: Protein | Mass: 20003.795 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NAA10, ARD1, ARD1A, TE2 / Production host: Homo sapiens (human)References: UniProt: P41227, N-terminal amino-acid Nalpha-acetyltransferase NatA |
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| #3: Protein | Mass: 98658.648 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NAA15, GA19, NARG1, NATH, TBDN100 / Production host: Homo sapiens (human) / References: UniProt: Q9BXJ9 |
-RNA chain , 2 types, 2 molecules 81
| #2: RNA chain | Mass: 50449.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) / References: GenBank: 1142736641 |
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| #4: RNA chain | Mass: 1640222.125 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
-60S ribosomal protein ... , 6 types, 6 molecules LCLkLhLXLRLr
| #5: Protein | Mass: 47804.621 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL4, RPL1 / Production host: Homo sapiens (human) / References: UniProt: P36578 |
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| #7: Protein | Mass: 8238.948 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL38 / Production host: Homo sapiens (human) / References: UniProt: P63173 |
| #9: Protein | Mass: 14462.429 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL35 / Production host: Homo sapiens (human) / References: UniProt: P42766 |
| #10: Protein | Mass: 17740.193 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL23A / Production host: Homo sapiens (human) / References: UniProt: P62750 |
| #11: Protein | Mass: 23535.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL19 / Production host: Homo sapiens (human) / References: UniProt: P84098 |
| #12: Protein | Mass: 15784.622 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL28 / Production host: Homo sapiens (human) / References: UniProt: P46779 |
-Large ribosomal subunit protein ... , 2 types, 2 molecules LELY
| #6: Protein | Mass: 32810.176 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL6, TXREB1 / Production host: Homo sapiens (human) / References: UniProt: Q02878 |
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| #8: Protein | Mass: 17174.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPL26 / Production host: Homo sapiens (human) / References: UniProt: P61254 |
-Protein / Non-polymers , 2 types, 2 molecules A

| #13: Protein | Mass: 43851.879 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PA2G4, EBP1 / Production host: Homo sapiens (human) / References: UniProt: Q9UQ80 |
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| #14: Chemical | ChemComp-KGN / |
-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: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: human 80S ribosome in complex with NatA and Ebp1 / Type: RIBOSOME / Entity ID: #1-#13 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Microscopy | Model: TFS GLACIOS |
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| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1700 nm / Nominal defocus min: 700 nm |
| Image recording | Electron dose: 51.65 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21_5207: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4.61 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 17235 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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Homo sapiens (human)
Germany, 1items
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