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Open data
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Basic information
Entry | Database: PDB / ID: 9kde | ||||||||||||||||||||||||||||||
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Title | Structure of 4n-bound TRPC3 at 3.3 angstrom | ||||||||||||||||||||||||||||||
![]() | Short transient receptor potential channel 3 | ||||||||||||||||||||||||||||||
![]() | METAL TRANSPORT / TRPC3 / DAG / MOG / 4n | ||||||||||||||||||||||||||||||
Function / homology | ![]() positive regulation of cardiac muscle hypertrophy in response to stress / Role of second messengers in netrin-1 signaling / store-operated calcium channel activity / Effects of PIP2 hydrolysis / Elevation of cytosolic Ca2+ levels / inositol 1,4,5 trisphosphate binding / calcium-activated cation channel activity / cation channel complex / TRP channels / response to ATP ...positive regulation of cardiac muscle hypertrophy in response to stress / Role of second messengers in netrin-1 signaling / store-operated calcium channel activity / Effects of PIP2 hydrolysis / Elevation of cytosolic Ca2+ levels / inositol 1,4,5 trisphosphate binding / calcium-activated cation channel activity / cation channel complex / TRP channels / response to ATP / positive regulation of calcium ion transport into cytosol / phototransduction / regulation of cytosolic calcium ion concentration / single fertilization / MECP2 regulates neuronal receptors and channels / response to calcium ion / calcium ion transmembrane transport / calcium channel activity / calcium ion transport / metal ion binding / plasma membrane Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.34 Å | ||||||||||||||||||||||||||||||
![]() | Chen, L. / Guo, W. / Chen, Y. / Zang, J. / Wei, M. | ||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of 4n-bound TRPC3 at 3.3 angstrom Authors: Chen, L. / Guo, W. / Chen, Y. / Zang, J. / Wei, M. | ||||||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 500 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 80.9 KB | Display | |
Data in CIF | ![]() | 120.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 62271MC 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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1 |
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Components
#1: Protein | Mass: 105662.812 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-A1L5Q / Mass: 448.438 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C22H23F3N4O3 / Feature type: SUBJECT OF INVESTIGATION Has ligand of interest | Y | Has protein modification | N | |
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-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: 4n-bound TRPC3 tetramer / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.5 |
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: 3000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 3.34 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 64003 / Symmetry type: POINT |