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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 | |||||||||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Short transient receptor potential channel 1 / Short transient receptor potential channel 5 | |||||||||||||||||||||
| Function / homology | Function and homology informationregulation 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 | ![]() ![]() ![]() Homo sapiens (human)![]() Human betaherpesvirus 5 | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.84 Å | |||||||||||||||||||||
Authors | Chen, Y.X. / Cheng, X.Y. / Zhang, J. | |||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: 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: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9k4i.cif.gz | 545.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9k4i.ent.gz | 410.7 KB | Display | PDB format |
| PDBx/mmJSON format | 9k4i.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9k4i_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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| Full document | 9k4i_full_validation.pdf.gz | 1.9 MB | Display | |
| Data in XML | 9k4i_validation.xml.gz | 92.2 KB | Display | |
| Data in CIF | 9k4i_validation.cif.gz | 134.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k4/9k4i ftp://data.pdbj.org/pub/pdb/validation_reports/k4/9k4i | 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 F&H Search |
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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: Homo sapiens (human) / References: UniProt: P0AEX9, UniProt: Q9QX29#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.) ![]() Homo sapiens (human), (gene. exp.) ![]() Human betaherpesvirus 5Gene: malE, b4034, JW3994, TRPC1, TRP1, UL32 / Production host: Homo sapiens (human)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: Homo sapiens (human) | ||||||||||||
| 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| 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 |
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About Yorodumi






Homo sapiens (human)
Human betaherpesvirus 5
Citation
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FIELD EMISSION GUN