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- PDB-9e7f: Cryo-EM structure of the Pyrobaculum calidifontis 70S ribosome in... -
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Open data
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Basic information
Entry | Database: PDB / ID: 9e7f | ||||||
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Title | Cryo-EM structure of the Pyrobaculum calidifontis 70S ribosome in complex with Dri | ||||||
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![]() | RIBOSOME / Translation / Hibernation / RNA | ||||||
Function / homology | ![]() ribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / maturation of SSU-rRNA / ribosome biogenesis / large ribosomal subunit / ribosomal small subunit assembly / ribosomal small subunit biogenesis / small ribosomal subunit ...ribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / maturation of SSU-rRNA / ribosome biogenesis / large ribosomal subunit / ribosomal small subunit assembly / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.53 Å | ||||||
![]() | Nissley, A.J. / Cate, J.H.D. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of an Archaeal Ribosome with a Divergent Active Site Authors: Nissley, A.J. / Shulgina, Y. / Kivimae, R.W. / Downing, B.E. / Penev, P.I. / Banfield, J.F. / Nayak, D.D. / Cate, J.H.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 4.3 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 268.9 KB | Display | |
Data in CIF | ![]() | 491.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 47668MC ![]() 9e6qC ![]() 9e71C C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-RNA chain , 3 types, 3 molecules 214
#1: RNA chain | Mass: 41803.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: GenBank: 126248349 |
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#3: RNA chain | Mass: 984007.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() |
#4: RNA chain | Mass: 487519.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: GenBank: 343200235 |
-Protein , 8 types, 8 molecules 3AMAeAhAjAkBbBc
#2: Protein | Mass: 72127.695 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MX58 |
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#16: Protein | Mass: 22623.768 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MWR6 |
#34: Protein | Mass: 7954.435 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MTT1 |
#37: Protein | Mass: 10603.610 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() |
#39: Protein | Mass: 20956.449 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MTM7 |
#40: Protein | Mass: 10938.797 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MWU0 |
#68: Protein | Mass: 7856.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() |
#69: Protein | Mass: 6956.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MY11 |
+Large ribosomal subunit protein ... , 31 types, 32 molecules AAABACADAEAFAGAHAIAJAKALANAOAPAQARASATAUAVAWAXAYAZAaAbAcAdAfAgAi
+Small ribosomal subunit protein ... , 24 types, 24 molecules BABBBCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBYBZ
-SSU ribosomal protein ... , 3 types, 3 molecules BWBXBa
#63: Protein | Mass: 12477.728 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MV37 |
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#64: Protein | Mass: 11571.864 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MV49 |
#67: Protein | Mass: 6113.139 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MSW3 |
-Non-polymers , 4 types, 6713 molecules 






#70: Chemical | ChemComp-SPM / #71: Chemical | ChemComp-MG / #72: Chemical | ChemComp-ZN / #73: Water | ChemComp-HOH / | |
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-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
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Molecular weight |
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Source (natural) |
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Buffer solution | pH: 7 | ||||||||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 0.12 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid type: UltrAuFoil R1.2/1.3 | ||||||||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 7318 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 2360632 | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.53 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 72157 / Details: Global resolution / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL |