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Open data
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Basic information
| Entry | Database: PDB / ID: 9o1j | ||||||||||||||||||||||||
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| Title | Pseudomonas aeruginosa ATPase State3 F1Fo focused | ||||||||||||||||||||||||
Components | (ATP synthase ...) x 8 | ||||||||||||||||||||||||
Keywords | ELECTRON TRANSPORT / ATPase / energy | ||||||||||||||||||||||||
| Function / homology | Function and homology informationproton motive force-driven plasma membrane ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton-transporting ATPase activity, rotational mechanism / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / lipid binding / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.02 Å | ||||||||||||||||||||||||
Authors | Stewart, A.G. / Sobti, M. | ||||||||||||||||||||||||
| Funding support | Australia, 1items
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Citation | Journal: To Be PublishedTitle: Distinct Structural Features of Pseudomonas aeruginosa ATP Synthase Revealed by Cryo Electron Microscopy Authors: Sobti, M. / Stewart, A.G. | ||||||||||||||||||||||||
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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 | 9o1j.cif.gz | 800 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9o1j.ent.gz | 664.5 KB | Display | PDB format |
| PDBx/mmJSON format | 9o1j.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9o1j_validation.pdf.gz | 2.1 MB | Display | wwPDB validaton report |
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| Full document | 9o1j_full_validation.pdf.gz | 2.1 MB | Display | |
| Data in XML | 9o1j_validation.xml.gz | 125.5 KB | Display | |
| Data in CIF | 9o1j_validation.cif.gz | 203.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o1/9o1j ftp://data.pdbj.org/pub/pdb/validation_reports/o1/9o1j | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 70009MC ![]() 9o19C ![]() 9o1aC ![]() 9o1bC ![]() 9o1cC ![]() 9o1dC ![]() 9o1eC ![]() 9o1fC ![]() 9o1gC ![]() 9o1hC ![]() 9o1kC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-ATP synthase ... , 8 types, 22 molecules ABCDEFGHIJLMNOPQRSWXYa
| #1: Protein | Mass: 55450.996 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: A6VF34, H+-transporting two-sector ATPase #2: Protein | Mass: 50380.129 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: A6VF32, H+-transporting two-sector ATPase #3: Protein | | Mass: 31593.328 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #4: Protein | | Mass: 14741.866 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #5: Protein | Mass: 8611.380 Da / Num. of mol.: 10 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #6: Protein | | Mass: 19283.980 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #7: Protein | Mass: 16978.346 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #8: Protein | | Mass: 31944.635 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 3 types, 11 molecules 




| #9: Chemical | | #10: Chemical | ChemComp-MG / #11: Chemical | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-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
| Component | Name: Pseudomonas aeruginosa ATPase / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % |
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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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 65 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
| 3D reconstruction | Resolution: 3.02 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 25274 / Symmetry type: POINT |
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FIELD EMISSION GUN