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Open data
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Basic information
Entry | Database: PDB / ID: 6f0n | ||||||
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Title | GLIC mutant E82A | ||||||
![]() | Proton-gated ion channel | ||||||
![]() | MEMBRANE PROTEIN / TRANSPORT PROTEIN | ||||||
Function / homology | ![]() sodium channel activity / extracellular ligand-gated monoatomic ion channel activity / potassium channel activity / transmembrane transporter complex / regulation of membrane potential / transmembrane signaling receptor activity / neuron projection / signal transduction / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hu, H.D. / Delarue, M. | ||||||
![]() | ![]() Title: Full mutational mapping of titratable residues helps to identify proton-sensors involved in the control of channel gating in the Gloeobacter violaceus pentameric ligand-gated ion channel. Authors: Nemecz, A. / Hu, H. / Fourati, Z. / Van Renterghem, C. / Delarue, M. / Corringer, 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 | ![]() | 654.2 KB | Display | ![]() |
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PDB format | ![]() | 547 KB | 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 | ![]() | 56.6 KB | Display | |
Data in CIF | ![]() | 75.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6f0iC ![]() 6f0jC ![]() 6f0mC ![]() 6f0rC ![]() 6f0uC ![]() 6f0vC ![]() 6f0zC ![]() 6f10C ![]() 6f11C ![]() 6f12C ![]() 6f13C ![]() 6f15C ![]() 6f16C C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein / Sugars , 2 types, 11 molecules ABCDE![](data/chem/img/LMT.gif)
![](data/chem/img/LMT.gif)
#1: Protein | Mass: 36219.688 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #6: Sugar | ChemComp-LMT / |
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-Non-polymers , 5 types, 130 molecules ![](data/chem/img/ACT.gif)
![](data/chem/img/PLC.gif)
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![](data/chem/img/HOH.gif)
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![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ACT / #3: Chemical | ChemComp-PLC / #4: Chemical | ChemComp-CL / #5: Chemical | ChemComp-NA / #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.14 Å3/Da / Density % sol: 76.06 % |
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Crystal grow | Temperature: 293 K / Method: evaporation Details: 12% PEG4K, 15% glycerol, 100 mM Acetate de Sodium pH4, 400 mM Sodium isothiocyanate, 3% DMSO |
-Data collection
Diffraction | Mean temperature: 190 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 6, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9194 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→49.31 Å / Num. obs: 60439 / % possible obs: 99.7 % / Redundancy: 3.9 % / Biso Wilson estimate: 85.95 Å2 / Net I/σ(I): 8.5 |
Reflection shell | Resolution: 3.2→3.28 Å |
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Processing
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Refinement | Resolution: 3.2→25 Å / Cor.coef. Fo:Fc: 0.8932 / Cor.coef. Fo:Fc free: 0.8591 / SU R Cruickshank DPI: 0.851 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.7 / SU Rfree Blow DPI: 0.33 / SU Rfree Cruickshank DPI: 0.346
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Displacement parameters | Biso mean: 78.04 Å2
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Refine analyze | Luzzati coordinate error obs: 0.451 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 3.2→25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.2→3.28 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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