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Open data
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Basic information
| Entry | Database: PDB / ID: 4v7l | |||||||||
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| Title | The structures of viomycin bound to the 70S ribosome. | |||||||||
Components |
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Keywords | RIBOSOME/ANTIBIOTIC / Anti-tuberculosis antibiotic / 70S / ribosome / tRNA / mRNA / tuberactinomycin / viomycin / RIBOSOME-Antibiotic complex | |||||||||
| Function / homology | Function and homology informationregulation of translation / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding ...regulation of translation / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() ![]() Thermus thermophilus (bacteria) Streptomyces puniceus (bacteria) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3 Å | |||||||||
Authors | Stanley, R.E. / Blaha, G. | |||||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2010Title: The structures of the anti-tuberculosis antibiotics viomycin and capreomycin bound to the 70S ribosome. Authors: Stanley, R.E. / Blaha, G. / Grodzicki, R.L. / Strickler, M.D. / Steitz, T.A. | |||||||||
| 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 | 4v7l.cif.gz | 7.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v7l.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v7l.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v7l_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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| Full document | 4v7l_full_validation.pdf.gz | 4.3 MB | Display | |
| Data in XML | 4v7l_validation.xml.gz | 1.1 MB | Display | |
| Data in CIF | 4v7l_validation.cif.gz | 1.4 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v7/4v7l ftp://data.pdbj.org/pub/pdb/validation_reports/v7/4v7l | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
-RNA chain , 7 types, 14 molecules AACAAVCVAWCWAXCXAYCYBADABBDB
| #1: RNA chain | Mass: 489961.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: AP008226.1#22: RNA chain | Mass: 9684.905 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: mRNA #23: RNA chain | Mass: 24060.287 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: A-site tRNA Gln / Source: (gene. exp.) ![]() ![]() #24: RNA chain | Mass: 24802.785 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: P-site tRNA fMet / Source: (gene. exp.) ![]() ![]() #25: RNA chain | Mass: 24077.270 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: E-site tRNA Gln / Source: (gene. exp.) ![]() ![]() #27: RNA chain | Mass: 947895.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: AP008226.1#28: RNA chain | Mass: 39494.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: GenBank: AP008226.1 |
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-30S ribosomal protein ... , 20 types, 40 molecules ABCBACCCADCDAECEAFCFAGCGAHCHAICIAJCJAKCKALCLAMCMANCNAOCOAPCP...
| #2: Protein | Mass: 29317.703 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80371#3: Protein | Mass: 26751.076 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80372#4: Protein | Mass: 24373.447 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80373#5: Protein | Mass: 17583.416 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHQ5#6: Protein | Mass: 11988.753 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SLP8#7: Protein | Mass: 18050.973 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P17291#8: Protein | Mass: 15868.570 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHQ2, UniProt: A0A0M9AFS9*PLUS#9: Protein | Mass: 14410.614 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80374#10: Protein | Mass: 11954.968 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHN7#11: Protein | Mass: 13737.868 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80376#12: Protein | Mass: 14637.384 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHN3#13: Protein | Mass: 14338.861 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80377#14: Protein | Mass: 7158.725 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHQ1, UniProt: A0A0N0BLP2*PLUS#15: Protein | Mass: 10578.407 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SJ76#16: Protein | Mass: 10409.983 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SJH3#17: Protein | Mass: 12325.655 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHP7, UniProt: A0A0N0BLS5*PLUS#18: Protein | Mass: 10258.299 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SLQ0#19: Protein | Mass: 10605.464 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SHP2#20: Protein | Mass: 11736.143 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: P80380#21: Protein/peptide | Mass: 3350.030 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() Thermus thermophilus (bacteria) / Strain: HB8 / References: UniProt: Q5SIH3 |
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-Protein/peptide , 1 types, 2 molecules AZCZ
| #26: Protein/peptide |
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+50S ribosomal protein ... , 30 types, 60 molecules BCDCBDDDBEDEBFDFBGDGBHDHBIDIBNDNBODOBPDPBQDQBRDRBSDSBTDTBUDU...
-Non-polymers , 2 types, 973 molecules 


| #59: Chemical | ChemComp-MG / #60: Chemical | ChemComp-ZN / |
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-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.29 Å3/Da / Density % sol: 62.56 % |
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| Crystal grow | Temperature: 292 K / Method: vapor diffusion / pH: 7.6 Details: 0.1-0.2 M Arginine-HCL, 0.1 M Tris pH 7.6, 2.5% Peg 20K, 7-12% MPD, 0.5 mM BME, vapor diffusion, temperature 292K |
-Data collection
| Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97949 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 4, 2008 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Monochromator: Kohzu HLD8-24 monochromator / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 0.97949 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 3→50 Å / Num. obs: 1121164 / % possible obs: 95.1 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 80.997 Å2 / Rmerge(I) obs: 0.307 / Net I/σ(I): 3.86 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell |
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-Phasing
| Phasing | Method: molecular replacement |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→50 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.807
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| Displacement parameters | Biso max: 200 Å2 / Biso mean: 94.291 Å2 / Biso min: 16.65 Å2 | ||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3→50 Å
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Thermus thermophilus (bacteria)
X-RAY DIFFRACTION
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