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Yorodumi- PDB-21tq: The structure of Nav1.7 with veratridine standing near the IFM mo... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 21tq | |||||||||||||||||||||
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| Title | The structure of Nav1.7 with veratridine standing near the IFM motif (site I) | |||||||||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Nav1.7 / voltage gated sodium channel / cryo-EM / veratridine / site I | |||||||||||||||||||||
| Function / homology | Function and homology informationresponse to pyrethroid / corticospinal neuron axon guidance / positive regulation of voltage-gated sodium channel activity / action potential propagation / detection of mechanical stimulus involved in sensory perception / voltage-gated sodium channel activity involved in cardiac muscle cell action potential / regulation of atrial cardiac muscle cell membrane depolarization / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / membrane depolarization during Purkinje myocyte cell action potential / cardiac conduction ...response to pyrethroid / corticospinal neuron axon guidance / positive regulation of voltage-gated sodium channel activity / action potential propagation / detection of mechanical stimulus involved in sensory perception / voltage-gated sodium channel activity involved in cardiac muscle cell action potential / regulation of atrial cardiac muscle cell membrane depolarization / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / membrane depolarization during Purkinje myocyte cell action potential / cardiac conduction / membrane depolarization during cardiac muscle cell action potential / membrane depolarization during action potential / positive regulation of sodium ion transport / regulation of sodium ion transmembrane transport / axon initial segment / regulation of ventricular cardiac muscle cell membrane repolarization / cardiac muscle cell action potential involved in contraction / node of Ranvier / voltage-gated sodium channel complex / sodium channel inhibitor activity / neuronal action potential propagation / locomotion / Interaction between L1 and Ankyrins / voltage-gated sodium channel activity / detection of temperature stimulus involved in sensory perception of pain / Phase 0 - rapid depolarisation / regulation of heart rate by cardiac conduction / behavioral response to pain / intercalated disc / sodium channel regulator activity / membrane depolarization / neuronal action potential / cardiac muscle contraction / T-tubule / sensory perception of pain / axon terminus / axon guidance / sodium ion transmembrane transport / post-embryonic development / circadian rhythm / positive regulation of neuron projection development / response to toxic substance / Sensory perception of sweet, bitter, and umami (glutamate) taste / nervous system development / response to heat / gene expression / chemical synaptic transmission / perikaryon / transmembrane transporter binding / cell adhesion / inflammatory response / axon / synapse / extracellular region / plasma membrane Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||||||||||||||
Authors | Fan, X. / Huang, J. / Yan, N. | |||||||||||||||||||||
| Funding support | France, 1items
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Citation | Journal: To Be PublishedTitle: Open-state structure of veratridine-activated human Nav1.7 reveals the molecular choreography of fast inactivation Authors: Fan, X. / Chen, J. / Xue, L. / Wang, H. / Wu, T. / Huang, X. / Lu, F. / Jin, X. / Song, C. / Huang, J. / Yan, N. | |||||||||||||||||||||
| History |
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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 | 21tq.cif.gz | 358.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb21tq.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 21tq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1t/21tq ftp://data.pdbj.org/pub/pdb/validation_reports/1t/21tq | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 67991MC 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
-Sodium channel regulatory subunit beta- ... , 2 types, 2 molecules BC
| #1: Protein | Mass: 20206.018 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SCN1B / Production host: Homo sapiens (human) / References: UniProt: Q07699 |
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| #2: Protein | Mass: 13965.937 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SCN2B, UNQ326/PRO386 / Production host: Homo sapiens (human) / References: UniProt: O60939 |
-Protein , 1 types, 1 molecules A
| #3: Protein | Mass: 226620.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SCN9A, NENA / Production host: Homo sapiens (human) / References: UniProt: Q15858 |
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-Sugars , 2 types, 8 molecules 
| #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Sugar | ChemComp-NAG / |
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-Non-polymers , 5 types, 16 molecules 






| #6: Chemical | ChemComp-LPE / #7: Chemical | ChemComp-A1E26 / | Mass: 673.790 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C36H51NO11 / Feature type: SUBJECT OF INVESTIGATION #8: Chemical | ChemComp-Y01 / #9: Chemical | #10: Chemical | ChemComp-P3X / ( | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-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: Nav1.7-veratridine complex / Type: COMPLEX / Entity ID: #1-#3 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| EM software |
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| Image processing |
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| CTF correction |
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| 3D reconstruction |
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| Refinement | Highest resolution: 2.7 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
France, 1items
Citation
PDBj






FIELD EMISSION GUN