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- PDB-8v64: RCK1-RCK2 double mutant of human Slo1 in presence of EDTA - resti... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8v64 | |||||||||||||||||||||||||||
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Title | RCK1-RCK2 double mutant of human Slo1 in presence of EDTA - resting VSD | |||||||||||||||||||||||||||
![]() | Calcium-activated potassium channel subunit alpha-1 | |||||||||||||||||||||||||||
![]() | TRANSPORT PROTEIN / Slo1 / BK / maxiK / potassium channel / voltage sensor / VSD / resting state | |||||||||||||||||||||||||||
Function / homology | ![]() Acetylcholine inhibits contraction of outer hair cells / micturition / Ca2+ activated K+ channels / large conductance calcium-activated potassium channel activity / calcium-activated potassium channel activity / negative regulation of cell volume / smooth muscle contraction involved in micturition / response to carbon monoxide / Sensory processing of sound by inner hair cells of the cochlea / response to osmotic stress ...Acetylcholine inhibits contraction of outer hair cells / micturition / Ca2+ activated K+ channels / large conductance calcium-activated potassium channel activity / calcium-activated potassium channel activity / negative regulation of cell volume / smooth muscle contraction involved in micturition / response to carbon monoxide / Sensory processing of sound by inner hair cells of the cochlea / response to osmotic stress / cGMP effects / intracellular potassium ion homeostasis / voltage-gated potassium channel activity / voltage-gated potassium channel complex / potassium ion transmembrane transport / regulation of membrane potential / response to calcium ion / caveola / potassium ion transport / vasodilation / actin binding / postsynaptic membrane / response to hypoxia / apical plasma membrane / positive regulation of apoptotic process / metal ion binding / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||||||||||||||||||||
![]() | Pal, K. / Kallure, G.S. / Chowdhury, S. | |||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: RCK1-RCK2 double mutant of human Slo1 in presence of EDTA - resting VSD Authors: Pal, K. / Kallure, G.S. / Chowdhury, S. | |||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 800 KB | Display | ![]() |
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PDB format | ![]() | 649.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.4 MB | Display | ![]() |
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Full document | ![]() | 3.4 MB | Display | |
Data in XML | ![]() | 104.4 KB | Display | |
Data in CIF | ![]() | 155.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 42989MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 119724.016 Da / Num. of mol.: 4 / Mutation: D894A,D895A,D896A,D897A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 5 types, 77 molecules 








#2: Chemical | ChemComp-K / #3: Chemical | ChemComp-POV / ( #4: Chemical | ChemComp-CLR / #5: Chemical | ChemComp-AJP / #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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Has protein modification | N |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: human Slo1 channel RCK1 RCK2 site double mutant in present of EDTA and in digitonin micelles Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1700 nm / Nominal defocus min: 900 nm |
Image recording | Electron dose: 72 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 612845 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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