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Open data
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Basic information
| Entry | Database: PDB / ID: 4v9p | |||||||||
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| Title | Control of ribosomal subunit rotation by elongation factor G | |||||||||
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Keywords | ribosome/antibiotic / Protein biosynthesis / ribosome / RNA / EF-G / elongation / factor / GTP / GDPCP / viomycin / tRNA / tranlocation / exit / peptidyl / 50S / 70S / 23S / ribosomal subunit / ribosome-antibiotic complex | |||||||||
| Function / homology | Function and homology informationribosome disassembly / guanosine tetraphosphate binding / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / translational elongation / misfolded RNA binding / Group I intron splicing / RNA folding / translation elongation factor activity ...ribosome disassembly / guanosine tetraphosphate binding / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / translational elongation / misfolded RNA binding / Group I intron splicing / RNA folding / translation elongation factor activity / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / regulation of mRNA stability / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / response to reactive oxygen species / ribosome assembly / transcription elongation factor complex / DNA endonuclease activity / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / large ribosomal subunit / ribosome biogenesis / ribosome binding / 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 / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / GTPase activity / mRNA binding / GTP binding / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() Streptomyces (bacteria) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.9 Å | |||||||||
Authors | Pulk, A. / Cate, J.H.D. | |||||||||
Citation | Journal: Science / Year: 2013Title: Control of ribosomal subunit rotation by elongation factor G. Authors: Pulk, A. / Cate, J.H. | |||||||||
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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 | 4v9p.cif.gz | 14.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v9p.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v9p.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v9p_validation.pdf.gz | 2.2 MB | Display | wwPDB validaton report |
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| Full document | 4v9p_full_validation.pdf.gz | 3.8 MB | Display | |
| Data in XML | 4v9p_validation.xml.gz | 866.1 KB | Display | |
| Data in CIF | 4v9p_validation.cif.gz | 1.4 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v9/4v9p ftp://data.pdbj.org/pub/pdb/validation_reports/v9/4v9p | 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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| 3 | ![]()
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| 4 | ![]()
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| Unit cell |
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Components
-RNA chain , 3 types, 12 molecules AACAEAGAABCBEBGBBADAFAHA
| #1: RNA chain | Mass: 941612.375 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #2: RNA chain | Mass: 38790.090 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #33: RNA chain | Mass: 499690.031 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() |
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+50S ribosomal protein ... , 30 types, 118 molecules ACCCECGCADCDEDGDAECEEEGEAFCFEFGFAGCGEGGGAHCHEHGHAICIEIGIAJCJ...
-30S ribosomal protein ... , 20 types, 80 molecules BBDBFBHBBCDCFCHCBDDDFDHDBEDEFEHEBFDFFFHFBGDGFGHGBHDHFHHHBIDI...
| #34: Protein | Mass: 26781.670 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #35: Protein | Mass: 26031.316 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #36: Protein | Mass: 23514.199 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #37: Protein | Mass: 17629.398 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #38: Protein | Mass: 15727.512 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #39: Protein | Mass: 20055.156 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #40: Protein | Mass: 14146.557 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #41: Protein | Mass: 14886.270 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #42: Protein | Mass: 11755.597 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #43: Protein | Mass: 13870.975 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #44: Protein | Mass: 13768.157 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #45: Protein | Mass: 13128.467 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #46: Protein | Mass: 11606.560 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #47: Protein | Mass: 10290.816 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #48: Protein | Mass: 9207.572 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #49: Protein | Mass: 9724.491 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #50: Protein | Mass: 9005.472 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #51: Protein | Mass: 10455.355 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #52: Protein | Mass: 9708.464 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #53: Protein | Mass: 8524.039 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein / Protein/peptide , 2 types, 7 molecules BVDVFVHVBWDWFW
| #54: Protein | Mass: 77676.227 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #55: Protein/peptide | |
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-Non-polymers , 4 types, 4224 molecules 






| #56: Chemical | ChemComp-MG / #57: Chemical | ChemComp-ZN / #58: Chemical | ChemComp-GCP / #59: Water | ChemComp-HOH / | |
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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: 24 |
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Sample preparation
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-Data collection
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| Radiation |
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| Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 | |||||||||||||||
| Reflection | Resolution: 2.9→70 Å / Num. obs: 1984536 / % possible obs: 89.6 % / Observed criterion σ(F): 0.58 / Observed criterion σ(I): 0.58 |
-Phasing
| Phasing | Method: molecular replacement |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→70 Å / Occupancy max: 1 / Occupancy min: 0.89 / σ(F): 0.58 Details: Zero B values occur for some waters due to scaling from the use of bulk solvent correction in the refinement
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| Displacement parameters | Biso max: 145.92 Å2 / Biso mean: 32.7421 Å2 / Biso min: 0 Å2 | ||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.9→70 Å
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