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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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![]() | 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 | ![]() ribosome disassembly / guanosine tetraphosphate binding / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / translational elongation / transcriptional attenuation ...ribosome disassembly / guanosine tetraphosphate binding / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / translational elongation / transcriptional attenuation / translation elongation factor activity / positive regulation of ribosome biogenesis / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / negative regulation of translational initiation / regulation of mRNA stability / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / ribosome assembly / transcription elongation factor complex / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / DNA endonuclease activity / response to reactive oxygen species / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / response to radiation / mRNA 5'-UTR binding / regulation of translation / ribosome biogenesis / large ribosomal subunit / ribosome binding / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / GTPase activity / negative regulation of DNA-templated transcription / mRNA binding / GTP binding / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm 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 | ![]() | 2.2 MB | Display | ![]() |
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Full document | ![]() | 3.8 MB | Display | |
Data in XML | ![]() | 866.1 KB | Display | |
Data in CIF | ![]() | 1.4 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 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: ![]() |
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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: 1984536 / % possible obs: 89.6 % / Observed criterion σ(F): 0.58 / Observed criterion σ(I): 0.58 |
-Phasing
Phasing | Method: ![]() |
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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: 145.92 Å2 / Biso mean: 32.7421 Å2 / Biso min: 0 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→70 Å
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