+Open data
-Basic information
Entry | Database: PDB / ID: 4wfg | ||||||
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Title | Human TRAAK K+ channel in a Tl+ bound conductive conformation | ||||||
Components |
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Keywords | METAL TRANSPORT / Mechanosensitive ion channel / two-pore domain potassium ion channel / membrane protein | ||||||
Function / homology | Function and homology information mechanosensitive potassium channel activity / TWIK related potassium channel (TREK) / temperature-gated cation channel activity / sensory perception of temperature stimulus / detection of mechanical stimulus involved in sensory perception of touch / Phase 4 - resting membrane potential / potassium channel complex / cellular response to alkaline pH / stabilization of membrane potential / potassium ion leak channel activity ...mechanosensitive potassium channel activity / TWIK related potassium channel (TREK) / temperature-gated cation channel activity / sensory perception of temperature stimulus / detection of mechanical stimulus involved in sensory perception of touch / Phase 4 - resting membrane potential / potassium channel complex / cellular response to alkaline pH / stabilization of membrane potential / potassium ion leak channel activity / cellular response to temperature stimulus / outward rectifier potassium channel activity / cellular response to fatty acid / potassium channel activity / potassium ion transmembrane transport / sensory perception of pain / potassium ion transport / memory / cellular response to mechanical stimulus / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Brohawn, S.G. / MacKinnon, R. | ||||||
Citation | Journal: Nature / Year: 2014 Title: Physical mechanism for gating and mechanosensitivity of the human TRAAK K+ channel. Authors: Brohawn, S.G. / Campbell, E.B. / MacKinnon, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4wfg.cif.gz | 548.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4wfg.ent.gz | 454.8 KB | Display | PDB format |
PDBx/mmJSON format | 4wfg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4wfg_validation.pdf.gz | 480.8 KB | Display | wwPDB validaton report |
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Full document | 4wfg_full_validation.pdf.gz | 504.2 KB | Display | |
Data in XML | 4wfg_validation.xml.gz | 49.4 KB | Display | |
Data in CIF | 4wfg_validation.cif.gz | 68.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wf/4wfg ftp://data.pdbj.org/pub/pdb/validation_reports/wf/4wfg | HTTPS FTP |
-Related structure data
Related structure data | 4wfeC 4wffC 4wfhC 4i9wS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Refine code: _
NCS ensembles :
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 32569.650 Da / Num. of mol.: 2 / Mutation: N104Q, N108Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCNK4, TRAAK / Production host: Komagataella pastoris (fungus) / References: UniProt: Q9NYG8 |
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-Antibody , 2 types, 4 molecules DFEG
#2: Antibody | Mass: 23038.404 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) #3: Antibody | Mass: 23474.381 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) |
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-Non-polymers , 3 types, 201 molecules
#4: Chemical | ChemComp-TL / #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.4 Å3/Da / Density % sol: 63.86 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.8 Details: 50 MM TRIS PH 8.8, 200 MM CA(NO3)2, 27-30%(VOL/VOL) PEG400, 52 MM TRICHLOROETHANOL PH range: 8-9 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9781 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 19, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9781 Å / Relative weight: 1 |
Reflection | Resolution: 3→48 Å / Num. obs: 40099 / % possible obs: 99.6 % / Redundancy: 5.6 % / Net I/σ(I): 14.7 |
Reflection shell | Resolution: 3→3.05 Å / Redundancy: 5.7 % / Mean I/σ(I) obs: 0.9 / % possible all: 99.7 |
-Processing
Software | Name: REFMAC / Version: 5.8.0073 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4I9w Resolution: 3→48 Å / Cor.coef. Fo:Fc: 0.91 / Cor.coef. Fo:Fc free: 0.916 / SU B: 43.04 / SU ML: 0.376 / Cross valid method: THROUGHOUT / ESU R Free: 0.371 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 108.712 Å2
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Refinement step | Cycle: 1 / Resolution: 3→48 Å
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Refine LS restraints |
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