+Open data
-Basic information
Entry | Database: PDB / ID: 4wff | ||||||
---|---|---|---|---|---|---|---|
Title | Human TRAAK K+ channel in a K+ bound nonconductive conformation | ||||||
Components |
| ||||||
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) / detection of mechanical stimulus involved in sensory perception of touch / Phase 4 - resting membrane potential / temperature-gated cation channel activity / sensory perception of temperature stimulus / 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) / detection of mechanical stimulus involved in sensory perception of touch / Phase 4 - resting membrane potential / temperature-gated cation channel activity / sensory perception of temperature stimulus / 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 / sensory perception of pain / potassium ion transmembrane transport / memory / potassium ion transport / 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: 2.5 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4wff.cif.gz | 546.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4wff.ent.gz | 452.4 KB | Display | PDB format |
PDBx/mmJSON format | 4wff.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wf/4wff ftp://data.pdbj.org/pub/pdb/validation_reports/wf/4wff | HTTPS FTP |
---|
-Related structure data
Related structure data | 4wfeC 4wfgC 4wfhC 4i9wS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Unit cell |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Refine code: 0
NCS ensembles :
|
-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 |
---|
-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) |
---|
-Non-polymers , 4 types, 192 molecules
#4: Chemical | ChemComp-K / #5: Chemical | #6: Chemical | ChemComp-D10 / | #7: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 3.41 Å3/Da / Density % sol: 63.88 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.8 Details: 50 mM TRIS PH 8.8, 200 mM CaCl2, 27-30% (vol/vol) PEG400 PH range: 8-9 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.0332 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 7, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→48.1 Å / Num. obs: 68997 / % possible obs: 98.9 % / Redundancy: 10.1 % / Net I/σ(I): 34.8 |
Reflection shell | Resolution: 2.5→2.54 Å / Redundancy: 10.3 % / Mean I/σ(I) obs: 1 / % possible all: 100 |
-Processing
Software | Name: REFMAC / Version: 5.8.0073 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4I9W Resolution: 2.5→48.1 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.94 / SU B: 29.468 / SU ML: 0.282 / Cross valid method: THROUGHOUT / ESU R: 0.342 / ESU R Free: 0.245 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 98.23 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 2.5→48.1 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|