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Yorodumi- PDB-7m5d: Cryo-EM structure of a non-rotated E.coli 70S ribosome in complex... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7m5d | |||||||||||||||||||||
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| Title | Cryo-EM structure of a non-rotated E.coli 70S ribosome in complex with RF3-GTP, RF1 and P-tRNA (state I) | |||||||||||||||||||||
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Keywords | RIBOSOME / RF1 / RF3 / GTP | |||||||||||||||||||||
| Function / homology | Function and homology informationregulation of translational termination / translation release factor activity, codon specific / translation release factor activity, codon nonspecific / guanosine tetraphosphate binding / DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / large ribosomal subunit / transferase activity / small ribosomal subunit / 5S rRNA binding ...regulation of translational termination / translation release factor activity, codon specific / translation release factor activity, codon nonspecific / guanosine tetraphosphate binding / DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / large ribosomal subunit / transferase activity / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / GTPase activity / mRNA binding / GTP binding / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||||||||||||||
Authors | Zhang, J. | |||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of a non-rotated E.coli 70S ribosome in complex with RF3-GTP, RF1 and P-tRNA (state I) Authors: Zhang, J. | |||||||||||||||||||||
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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 | 7m5d.cif.gz | 3.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7m5d.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7m5d.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7m5d_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 7m5d_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML | 7m5d_validation.xml.gz | 244.7 KB | Display | |
| Data in CIF | 7m5d_validation.cif.gz | 417.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m5/7m5d ftp://data.pdbj.org/pub/pdb/validation_reports/m5/7m5d | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 23673MC 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
-RNA chain , 5 types, 5 molecules 12345
| #1: RNA chain | Mass: 941526.438 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: RNA chain | Mass: 497405.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: RNA chain | Mass: 38790.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: RNA chain | Mass: 4729.882 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
| #5: RNA chain | Mass: 24565.785 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+50S ribosomal protein ... , 31 types, 31 molecules BCDEFGJKLMNOPQRSTUVWXYZabcdefIH
-30S ribosomal protein ... , 20 types, 20 molecules ghijklmnopqrstuvwxyz
| #35: Protein | Mass: 25072.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #36: Protein | Mass: 23248.994 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: Protein | Mass: 23383.002 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #38: Protein | Mass: 16475.037 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #39: Protein | Mass: 12125.993 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #40: Protein | Mass: 16861.523 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #41: Protein | Mass: 14015.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #42: Protein | Mass: 14554.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 11254.041 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 12487.200 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #45: Protein | Mass: 13683.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #46: Protein | Mass: 12868.091 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #47: Protein | Mass: 11475.364 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #48: Protein | Mass: 10159.621 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #50: Protein | Mass: 9263.946 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #51: Protein | Mass: 7734.896 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #52: Protein | Mass: 9421.018 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #53: Protein | Mass: 9577.268 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #54: Protein | Mass: 8392.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Peptide chain release factor ... , 2 types, 2 molecules 7A
| #55: Protein | Mass: 58891.066 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #58: Protein | Mass: 40579.336 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein/peptide / Non-polymers , 2 types, 2 molecules 6

| #59: Protein/peptide | Mass: 471.569 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #60: Chemical | ChemComp-ZN / |
-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-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 |
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| Source (natural) |
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| 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
| 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 |
| Image recording | Electron dose: 30 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 86478 / Symmetry type: POINT |
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fluorescence resonance energy transfer
