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Yorodumi- PDB-25ii: Cryo-EM structure of human Nav1.6 in complex with Iota-Conotoxin RXIA -
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Open data
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Basic information
| Entry | Database: PDB / ID: 25ii | |||||||||||||||||||||||||||
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| Title | Cryo-EM structure of human Nav1.6 in complex with Iota-Conotoxin RXIA | |||||||||||||||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Nav1.6 / voltage gated sodium channel / cryo-EM / toxin / Iota-Conotoxin RXIA / TRANSPORT PROTEIN-TOXIN complex | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationcorticospinal neuron axon guidance / positive regulation of voltage-gated sodium channel activity / regulation of atrial cardiac muscle cell membrane depolarization / sodium ion binding / 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 / peripheral nervous system development ...corticospinal neuron axon guidance / positive regulation of voltage-gated sodium channel activity / regulation of atrial cardiac muscle cell membrane depolarization / sodium ion binding / 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 / peripheral nervous system development / regulation of sodium ion transmembrane transport / axon initial segment / regulation of ventricular cardiac muscle cell membrane repolarization / node of Ranvier / cardiac muscle cell action potential involved in contraction / sodium channel inhibitor activity / voltage-gated sodium channel complex / podosome / neuronal action potential propagation / locomotion / Interaction between L1 and Ankyrins / voltage-gated sodium channel activity / sodium ion transport / Phase 0 - rapid depolarisation / regulation of heart rate by cardiac conduction / intercalated disc / action potential / sodium channel regulator activity / membrane depolarization / cardiac muscle contraction / myelination / T-tubule / axon guidance / sodium ion transmembrane transport / positive regulation of neuron projection development / Z disc / Sensory perception of sweet, bitter, and umami (glutamate) taste / cell junction / toxin activity / cytoplasmic vesicle / perikaryon / transmembrane transporter binding / cell adhesion / axon / extracellular region / membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) Conus radiatus (invertebrata) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.5 Å | |||||||||||||||||||||||||||
Authors | Fan, X. / Huang, J. / Yan, N. | |||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: To Be PublishedTitle: Diverse modulation mechanisms of human Nav1.6 by gating modifier neurotoxins Authors: Fan, X. / Jian, H. / Yang, L. / Chen, J. / Wang, H. / Huang, X. / Geng, J. / Wu, Q. / Xie, Y. / Lu, F. / Guo, Q. / Shen, Z. / Jin, X. / Yan, N. | |||||||||||||||||||||||||||
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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 | 25ii.cif.gz | 348.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb25ii.ent.gz | 263.7 KB | Display | PDB format |
| PDBx/mmJSON format | 25ii.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/5i/25ii ftp://data.pdbj.org/pub/pdb/validation_reports/5i/25ii | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 80134MC ![]() 25ihC ![]() 9dk5C 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 ... , 2 types, 2 molecules AC
| #1: Protein | Mass: 225520.609 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SCN8A, MED / Production host: Homo sapiens (human) / References: UniProt: Q9UQD0 |
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| #2: Protein | Mass: 24732.115 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 |
-Protein/peptide , 1 types, 1 molecules D
| #3: Protein/peptide | Mass: 4987.667 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Conus radiatus (invertebrata) / Production host: Conus radiatus (invertebrata) / References: UniProt: Q7Z094 |
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-Sugars , 3 types, 9 molecules 
| #4: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose Type: oligosaccharide / Mass: 1559.386 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
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| #5: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
| #6: Sugar | ChemComp-NAG / |
-Non-polymers , 9 types, 42 molecules 
















| #7: Chemical | ChemComp-9Z9 / ( | ||||||||||||||
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| #8: Chemical | ChemComp-PCW / #9: Chemical | #10: Chemical | ChemComp-CLR / | #11: Chemical | ChemComp-P5S / | #12: Chemical | ChemComp-LPE / | #13: Chemical | ChemComp-P3X / ( | #14: Chemical | ChemComp-NA / | #15: Water | ChemComp-HOH / | |
-Details
| Has ligand of interest | N |
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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: Nav1.6-Iota-conotoxin RXIA / Type: COMPLEX / Entity ID: #1-#3 / Source: RECOMBINANT | ||||||||||||
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| Source (natural) |
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| Source (recombinant) |
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| 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: 1500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 179486 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.5 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
Conus radiatus (invertebrata)
China, 1items
Citation




PDBj












FIELD EMISSION GUN