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- PDB-8fbp: Glutamine synthetase from Pseudomonas aeruginosa, filament double... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8fbp | ||||||
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Title | Glutamine synthetase from Pseudomonas aeruginosa, filament double-unit in compressed conformation | ||||||
![]() | Glutamine synthetase | ||||||
![]() | LIGASE / glutamine biosynthetic process nitrogen utilization / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID | ||||||
Function / homology | ![]() nitrogen utilization / glutamine synthetase / glutamine biosynthetic process / glutamine synthetase activity / ATP binding / membrane / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å | ||||||
![]() | Phan, I.Q. / Staker, B. / Shek, R. / Moser, T.H. / Evans, J.E. / van Voorhis, W.C. / Myler, P.J. / Seattle Structural Genomics Center for Infectious Disease (SSGCID) | ||||||
Funding support | ![]()
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![]() | ![]() Title: Glutamine synthetase from Pseudomonas aeruginosa, filament double-unit in compressed conformation Authors: Phan, I.Q. / Staker, B. / Shek, R. / Moser, T.H. / Evans, J.E. / van Voorhis, W.C. / Myler, P.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.1 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 254.5 KB | Display | |
Data in CIF | ![]() | 394.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 28965MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 53039.711 Da / Num. of mol.: 28 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() References: UniProt: Q9HU65, glutamine synthetase |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: P. aeruginosa GS filament. / Type: COMPLEX / Details: Filament formation during sample preparation. / Entity ID: all / Source: RECOMBINANT | |||||||||||||||||||||||||
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Source (natural) | Organism: ![]() ![]() | |||||||||||||||||||||||||
Source (recombinant) | Organism: ![]() ![]() | |||||||||||||||||||||||||
Buffer solution | pH: 7 Details: Buffer components of purified protein, final vitrification diluted 50/50 with water. | |||||||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 300 nm / C2 aperture diameter: 50 µm |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
Software |
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EM software |
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CTF correction | Details: Patch-based motion correction / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C7 (7 fold cyclic) | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 346920 Details: CryoSPARC GSFSC: no mask 3.3A, loose 3.0A, tight 2.8A, corrected 2.8A. Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | B value: 62 / Protocol: FLEXIBLE FIT / Space: REAL / Target criteria: Cross-correlation coefficient | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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