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Open data
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Basic information
Entry | Database: PDB / ID: 9k4i | |||||||||||||||||||||
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Title | Cryo-EM structure of the human TRPC1/C5 heteromer | |||||||||||||||||||||
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![]() | MEMBRANE PROTEIN / Short transient receptor potential channel 1 / Short transient receptor potential channel 5 | |||||||||||||||||||||
Function / homology | ![]() regulation of membrane hyperpolarization / phosphatidylserine exposure on apoptotic cell surface / negative regulation of dendrite morphogenesis / Role of second messengers in netrin-1 signaling / store-operated calcium channel activity / viral tegument / melanin biosynthetic process / TRP channels / inositol 1,4,5 trisphosphate binding / cation channel complex ...regulation of membrane hyperpolarization / phosphatidylserine exposure on apoptotic cell surface / negative regulation of dendrite morphogenesis / Role of second messengers in netrin-1 signaling / store-operated calcium channel activity / viral tegument / melanin biosynthetic process / TRP channels / inositol 1,4,5 trisphosphate binding / cation channel complex / actinin binding / TRP channels / clathrin binding / detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / regulation of cardiac conduction / maltose transport / maltodextrin transmembrane transport / regulation of cytosolic calcium ion concentration / positive regulation of axon extension / monoatomic cation channel activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / Ion homeostasis / calcium channel complex / positive regulation of neuron differentiation / ATP-binding cassette (ABC) transporter complex / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / positive regulation of release of sequestered calcium ion into cytosol / bioluminescence / cell chemotaxis / generation of precursor metabolites and energy / response to calcium ion / calcium ion transmembrane transport / calcium channel activity / neuron differentiation / calcium ion transport / presynapse / outer membrane-bounded periplasmic space / actin binding / positive regulation of cytosolic calcium ion concentration / growth cone / ATPase binding / neuron apoptotic process / transmembrane transporter binding / periplasmic space / receptor complex / signaling receptor binding / neuronal cell body / positive regulation of cell population proliferation / dendrite / DNA damage response / structural molecule activity / membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.84 Å | |||||||||||||||||||||
![]() | Chen, Y.X. / Cheng, X.Y. / Zhang, J. | |||||||||||||||||||||
Funding support | 1items
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![]() | ![]() Title: Cryo-EM structure of the human TRPC1/C5 heteromer Authors: Chen, Y.X. / Cheng, X.Y. | |||||||||||||||||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 545.9 KB | Display | ![]() |
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PDB format | ![]() | 410.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
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Full document | ![]() | 1.9 MB | Display | |
Data in XML | ![]() | 92.2 KB | Display | |
Data in CIF | ![]() | 134.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 62060MC 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
#1: Protein | Mass: 136984.219 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: Flag-Flag-Flag-MBP-mTRPC5 Source: (gene. exp.) ![]() ![]() ![]() ![]() Gene: malE, b4034, JW3994, Trpc5, Trp5, Trrp5 / Production host: ![]() #2: Protein | | Mass: 168800.609 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: MBP-hTRPC1-GFP-Strep-Strep Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() Gene: malE, b4034, JW3994, TRPC1, TRP1, UL32 / Production host: ![]() References: UniProt: P0AEX9, UniProt: P48995, UniProt: A0A076JQ90 #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-YZY / ( Has ligand of interest | Y | Has protein modification | Y | |
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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: Cryo-EM structure of the human TRPC1/C5 heteromer / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT | ||||||||||||
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Source (natural) |
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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: Tecnai F30 / Image courtesy: FEI Company |
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Microscopy | Model: FEI TECNAI F30 |
Electron gun | Electron source: ![]() |
Electron lens | Mode: 4D-STEM / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 54 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 2.84 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 143788 / Symmetry type: POINT |