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Open data
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Basic information
Entry | Database: PDB / ID: 6cq6 | |||||||||
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Title | K2P2.1(TREK-1) apo structure | |||||||||
![]() | Potassium channel subfamily K member 2 | |||||||||
![]() | TRANSPORT PROTEIN / TREK-1 ion channel K2P | |||||||||
Function / homology | ![]() TWIK related potassium channel (TREK) / Phase 4 - resting membrane potential / positive regulation of cellular response to hypoxia / cardiac ventricle development / negative regulation of cardiac muscle cell proliferation / stabilization of membrane potential / potassium ion leak channel activity / astrocyte projection / potassium channel inhibitor activity / negative regulation of DNA biosynthetic process ...TWIK related potassium channel (TREK) / Phase 4 - resting membrane potential / positive regulation of cellular response to hypoxia / cardiac ventricle development / negative regulation of cardiac muscle cell proliferation / stabilization of membrane potential / potassium ion leak channel activity / astrocyte projection / potassium channel inhibitor activity / negative regulation of DNA biosynthetic process / outward rectifier potassium channel activity / cochlea development / voltage-gated potassium channel activity / calyx of Held / response to axon injury / response to mechanical stimulus / axon terminus / potassium ion transmembrane transport / voltage-gated potassium channel complex / regulation of membrane potential / potassium ion transport / memory / cellular response to hypoxia / G protein-coupled receptor signaling pathway / apical plasma membrane / axon / neuronal cell body / cell surface / endoplasmic reticulum / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Lolicato, M. / Minor, D.L. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: K2P2.1 (TREK-1)-activator complexes reveal a cryptic selectivity filter binding site. Authors: Lolicato, M. / Arrigoni, C. / Mori, T. / Sekioka, Y. / Bryant, C. / Clark, K.A. / Minor, D.L. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 129.5 KB | Display | ![]() |
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PDB format | ![]() | 99 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 467.5 KB | Display | ![]() |
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Full document | ![]() | 490.8 KB | Display | |
Data in XML | ![]() | 24.4 KB | Display | |
Data in CIF | ![]() | 31.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6cq8C ![]() 6cq9C ![]() 4rueS S: Starting model for refinement 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
#1: Protein | Mass: 34303.938 Da / Num. of mol.: 2 Mutation: K65R, Q66E, T67K, I69L, A70R, Q71A, A73P, N76S, S77D, T78Q, S281A, E287A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-K / #4: Chemical | ChemComp-D10 / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.89 Å3/Da / Density % sol: 68.35 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 22-25% PEG400, 100mM HEPES pH=8.0, 1mM CdCl2, 200mM KCl |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 3, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.115869 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→15 Å / Num. obs: 18913 / % possible obs: 97 % / Redundancy: 6 % / Rmerge(I) obs: 0.065 / Net I/σ(I): 0.3 |
Reflection shell | Resolution: 3.1→3.21 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.104 / Mean I/σ(I) obs: 0.3 / Num. unique obs: 2574 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4RUE Resolution: 3.1→14.965 Å / SU ML: 0.63 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 35.75
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→14.965 Å
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Refine LS restraints |
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LS refinement shell |
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