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Open data
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Basic information
Entry | Database: PDB / ID: 9g4y | ||||||||||||||||||||||||
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Title | TRPC5 in complex with photoswitch E-AzHC | ||||||||||||||||||||||||
![]() | Short transient receptor potential channel 5 | ||||||||||||||||||||||||
![]() | MEMBRANE PROTEIN / photo-switch / inhibitor | ||||||||||||||||||||||||
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 / inositol 1,4,5 trisphosphate binding / cation channel complex / actinin binding / TRP channels / clathrin binding ...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 / TRP channels / clathrin binding / regulation of cytosolic calcium ion concentration / positive regulation of axon extension / calcium channel complex / positive regulation of neuron differentiation / calcium ion transmembrane transport / calcium channel activity / neuron differentiation / calcium ion transport / nervous system development / presynapse / actin binding / positive regulation of cytosolic calcium ion concentration / ATPase binding / growth cone / neuron apoptotic process / neuronal cell body / positive regulation of cell population proliferation / dendrite / plasma membrane Similarity search - Function | ||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å | ||||||||||||||||||||||||
![]() | Porav, S.A. / Bon, R. / Muench, S. | ||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Ideal efficacy photoswitches for TRPC4/5 channels harness high potency for spatiotemporally-resolved control of TRPC function in live tissues Authors: Muller, M. / Niemeyer, K. / Ojha, N.K. / Porav, S.A. / Vinayagam, D. / Urban, N. / Buchau, F. / Oleinikov, K. / Makke, M. / Bauer, C.C. / Johnson, A.J. / Muench, S.P. / Zufall, F. / Bruns, D. ...Authors: Muller, M. / Niemeyer, K. / Ojha, N.K. / Porav, S.A. / Vinayagam, D. / Urban, N. / Buchau, F. / Oleinikov, K. / Makke, M. / Bauer, C.C. / Johnson, A.J. / Muench, S.P. / Zufall, F. / Bruns, D. / Schwarz, Y. / Raunser, S. / Leinders-Zufall, T. / Bon, R.S. / Schaefe, M. / Thorn-Seshold, O. | ||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 544.9 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 95.5 KB | Display | |
Data in CIF | ![]() | 139.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 51074MC ![]() 9g50C 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: 89065.922 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | ChemComp-A1IIE / Mass: 579.434 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C28H24Cl2N6O4 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: Homotetrameric TRPC5 ion channel in complex with a efficacy photo-switch, antagonist state. Type: CELL / Entity ID: #1 / Source: NATURAL | ||||||||||||||||||||
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Source (natural) | Organism: ![]() | ||||||||||||||||||||
Buffer solution | pH: 7.4 | ||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||
Vitrification | Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 277 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 165000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 700 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 35 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
EM software | Name: PHENIX / Version: 1.21rc1_5109: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 89351 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL / Space: REAL | ||||||||||||||||||||||||
Refine LS restraints |
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