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Open data
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Basic information
Entry | Database: PDB / ID: 4v9o | |||||||||
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Title | Control of ribosomal subunit rotation by elongation factor G | |||||||||
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![]() | Ribosome/antibiotic / Protein biosynthesis / ribosome / RNA / EF-G / elongation / factor / GTP / GDPCP / viomycin / tRNA / tranlocation / exit / peptidyl / 50S / 70S / 23S / ribosomal subunit / Elongation factor G / Ribosome-antibiotic complex | |||||||||
Function / homology | ![]() ribosome disassembly / translational elongation / guanosine tetraphosphate binding / stringent response / mRNA base-pairing translational repressor activity / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding ...ribosome disassembly / translational elongation / guanosine tetraphosphate binding / stringent response / mRNA base-pairing translational repressor activity / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / translation elongation factor activity / translational termination / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / regulation of mRNA stability / ribosome assembly / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / assembly of large subunit precursor of preribosome / transcription elongation factor complex / DNA endonuclease activity / regulation of DNA-templated transcription elongation / cytosolic ribosome assembly / transcription antitermination / response to reactive oxygen species / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / response to radiation / ribosomal large subunit assembly / mRNA 5'-UTR binding / large ribosomal subunit / ribosome biogenesis / ribosome binding / regulation of translation / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / transferase activity / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / tRNA binding / molecular adaptor activity / cytoplasmic translation / rRNA binding / negative regulation of translation / ribosome / structural constituent of ribosome / translation / response to antibiotic / GTPase activity / negative regulation of DNA-templated transcription / mRNA binding / GTP binding / protein homodimerization activity / DNA binding / RNA binding / zinc ion binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Pulk, A. / Cate, J.H.D. | |||||||||
![]() | ![]() Title: Control of ribosomal subunit rotation by elongation factor G. Authors: Pulk, A. / Cate, J.H. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 14.6 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.6 MB | Display | ![]() |
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Full document | ![]() | 5.3 MB | Display | |
Data in XML | ![]() | 1.4 MB | Display | |
Data in CIF | ![]() | 2.1 MB | Display | |
Arichive directory | ![]() ![]() | 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 ABCBEBGBAACAEAGABADAFAHA
#1: RNA chain | Mass: 38790.090 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: RNA chain | Mass: 941612.375 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #35: 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 ... , 31 types, 120 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) ![]() ![]() #36: Protein | Mass: 26031.316 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #37: Protein | Mass: 23514.199 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #38: Protein | Mass: 17629.398 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #39: Protein | Mass: 15727.512 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #40: Protein | Mass: 20055.156 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #41: Protein | Mass: 14146.557 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #42: Protein | Mass: 14886.270 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #43: Protein | Mass: 11755.597 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #44: Protein | Mass: 13870.975 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #45: Protein | Mass: 13768.157 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #46: Protein | Mass: 13128.467 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #47: Protein | Mass: 11606.560 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #48: Protein | Mass: 10290.816 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #49: Protein | Mass: 9207.572 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #50: Protein | Mass: 9724.491 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #51: Protein | Mass: 9005.472 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #52: Protein | Mass: 10455.355 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #53: Protein | Mass: 9708.464 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #54: 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, 8 molecules BVDVFVHVBWDWFWHW
#55: Protein | Mass: 77676.227 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #56: Protein/peptide | |
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-Non-polymers , 4 types, 4232 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/GCP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/GCP.gif)
![](data/chem/img/HOH.gif)
#57: Chemical | ChemComp-MG / #58: Chemical | ChemComp-ZN / #59: Chemical | ChemComp-GCP / #60: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal |
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-Data collection
Diffraction |
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Detector |
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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: 1874109 / % possible obs: 83.7 % / Observed criterion σ(F): 0.84 / Observed criterion σ(I): 0.84 |
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Processing
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Refinement | Method to determine structure: ![]() 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: 145.13 Å2 / Biso mean: 19.6361 Å2 / Biso min: 0 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→70 Å
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