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Yorodumi- PDB-9rsg: Human TRPC5 in complex with (-) englerin A, mixed occupancy_2, state 2 -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9rsg | |||||||||||||||||||||||||||||||||
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| Title | Human TRPC5 in complex with (-) englerin A, mixed occupancy_2, state 2 | |||||||||||||||||||||||||||||||||
Components | Short transient receptor potential channel 5 | |||||||||||||||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / TRPC5 / (-) englerin A / agonist | |||||||||||||||||||||||||||||||||
| 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 / inositol 1,4,5 trisphosphate binding / cation channel complex / actinin binding / clathrin binding / TRP channels ...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 / inositol 1,4,5 trisphosphate binding / cation channel complex / actinin binding / clathrin binding / TRP channels / positive regulation of axon extension / regulation of cytosolic calcium ion concentration / positive regulation of neuron differentiation / calcium channel complex / calcium ion transmembrane transport / calcium channel activity / neuron differentiation / calcium ion transport / nervous system development / ATPase binding / growth cone / presynapse / positive regulation of cytosolic calcium ion concentration / actin binding / neuron apoptotic process / neuronal cell body / positive regulation of cell population proliferation / dendrite / metal ion binding / plasma membrane Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||||||||||||||||||||||||||
Authors | Porav, A.S. / Bon, R.S. / Muench, S. | |||||||||||||||||||||||||||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: (-)-Englerin A binding to human TRPC5 exposes an aromatic interaction network in channel activation. Authors: Porav, S.A. / Ptakova, A. / Bauer, C.C. / Hammond, K.L.R. / Beech, D.J. / Vlachova, V. / Muench, S.P. / Bon, R.S. | |||||||||||||||||||||||||||||||||
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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 | 9rsg.cif.gz | 464.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9rsg.ent.gz | 380.4 KB | Display | PDB format |
| PDBx/mmJSON format | 9rsg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rs/9rsg ftp://data.pdbj.org/pub/pdb/validation_reports/rs/9rsg | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 54218 ![]() 9rrfC ![]() 9rrmC ![]() 9rrnC ![]() 9rroC ![]() 9rrqC ![]() 9rruC ![]() 9rshC ![]() 9rvvC 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: 89009.820 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TRPC5, TRP5 / Production host: Homo sapiens (human) / References: UniProt: Q9UL62#2: Chemical | ChemComp-ZN / Has ligand of interest | N | 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: Human TRPC5 in complex with (-) englerin A, mixed occupancy_2, state 2 Type: CELL / Entity ID: #1 / Source: NATURAL | ||||||||||||||||||||
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| Source (natural) | Organism: Homo sapiens (human) | ||||||||||||||||||||
| Buffer solution | pH: 7.4 | ||||||||||||||||||||
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| Specimen | Conc.: 0.9 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Homogeneous sample | ||||||||||||||||||||
| Specimen support | Grid type: Quantifoil | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 700 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 34.75 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 62384 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: AB INITIO MODEL / Space: REAL | ||||||||||||||||||||||||||||||||
| Atomic model building | Details: ModelAngelo / Source name: Other / Type: in silico model | ||||||||||||||||||||||||||||||||
| Refinement | Highest resolution: 3.2 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
United Kingdom, 1items
Citation








PDBj




FIELD EMISSION GUN