+Open data
-Basic information
Entry | Database: PDB / ID: 6cq8 | |||||||||
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Title | K2P2.1(TREK-1):ML335 complex | |||||||||
Components | Potassium channel subfamily K member 2 | |||||||||
Keywords | TRANSPORT PROTEIN / TREK-1 ion channel K2P | |||||||||
Function / homology | Function and homology information TWIK related potassium channel (TREK) / Phase 4 - resting membrane potential / positive regulation of cellular response to hypoxia / cardiac ventricle development / stabilization of membrane potential / potassium ion leak channel activity / negative regulation of cardiac muscle cell proliferation / astrocyte projection / potassium channel inhibitor activity / outward rectifier potassium channel activity ...TWIK related potassium channel (TREK) / Phase 4 - resting membrane potential / positive regulation of cellular response to hypoxia / cardiac ventricle development / stabilization of membrane potential / potassium ion leak channel activity / negative regulation of cardiac muscle cell proliferation / astrocyte projection / potassium channel inhibitor activity / outward rectifier potassium channel activity / negative regulation of DNA biosynthetic process / cochlea development / voltage-gated potassium channel activity / calyx of Held / response to axon injury / voltage-gated potassium channel complex / axon terminus / response to mechanical stimulus / potassium ion transmembrane transport / 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 | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | |||||||||
Authors | Lolicato, M. / Minor, D.L. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Nature / Year: 2017 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6cq8.cif.gz | 136 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6cq8.ent.gz | 103.2 KB | Display | PDB format |
PDBx/mmJSON format | 6cq8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cq/6cq8 ftp://data.pdbj.org/pub/pdb/validation_reports/cq/6cq8 | HTTPS FTP |
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-Related structure data
Related structure data | 6cq6C 6cq9C 4rueS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 34303.938 Da / Num. of mol.: 2 Mutation: K84R, Q85E, T86K, I88L, A89R, Q90A, A92P, N95S, S96D, T97Q, N119A, S300A, E306A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kcnk2 / Production host: Komagataella pastoris (fungus) / References: UniProt: P97438 |
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-Non-polymers , 5 types, 22 molecules
#2: Chemical | ChemComp-K / #3: Chemical | ChemComp-R16 / #4: Chemical | #5: Chemical | ChemComp-16C / | #6: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.74 Å3/Da / Density % sol: 67.11 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 20-25% PEG400 200mM KCl 1mM CdCl 100mM HEPES, pH=8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0332 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 21, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 3→15 Å / Num. obs: 21069 / % possible obs: 97 % / Redundancy: 12.9 % / Rmerge(I) obs: 0.237 / Net I/σ(I): 0.6 |
Reflection shell | Resolution: 3→3.11 Å / Rmerge(I) obs: 0.171 / Num. unique obs: 2724 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4RUE Resolution: 3→14.953 Å / SU ML: 0.55 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 33.55
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→14.953 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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