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Yorodumi- PDB-29tc: Cryo-EM structure of homo-hexameric hLRRC8A double mutation I2C/L402W -
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Open data
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Basic information
| Entry | Database: PDB / ID: 29tc | |||||||||
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| Title | Cryo-EM structure of homo-hexameric hLRRC8A double mutation I2C/L402W | |||||||||
Components | Volume-regulated anion channel subunit LRRC8A | |||||||||
Keywords | MEMBRANE PROTEIN / Volume-regulated anion channel subunit LRRC8A | |||||||||
| Function / homology | Function and homology informationpre-B cell differentiation / Miscellaneous transport and binding events / volume-sensitive anion channel activity / aspartate transmembrane transport / cyclic-GMP-AMP transmembrane transporter activity / cyclic-GMP-AMP transmembrane import across plasma membrane / monoatomic anion transmembrane transport / taurine transmembrane transport / cell volume homeostasis / monoatomic anion transport ...pre-B cell differentiation / Miscellaneous transport and binding events / volume-sensitive anion channel activity / aspartate transmembrane transport / cyclic-GMP-AMP transmembrane transporter activity / cyclic-GMP-AMP transmembrane import across plasma membrane / monoatomic anion transmembrane transport / taurine transmembrane transport / cell volume homeostasis / monoatomic anion transport / protein hexamerization / response to osmotic stress / monoatomic ion channel complex / positive regulation of myoblast differentiation / intracellular glucose homeostasis / chloride transmembrane transport / positive regulation of insulin secretion / spermatogenesis / lysosomal membrane / cell surface / membrane / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.54 Å | |||||||||
Authors | Bertelli, S. / Wang, L. / Klussendorf, M. / Pusch, M. / Dutzler, R. / Stauber, T. | |||||||||
| Funding support | Switzerland, 1items
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Citation | Journal: To Be Published / Year: 2026Title: The intracellular subdomain of the volume regulated anion channel subunit LRRC8A is a hotspot of channel activation Authors: Bertelli, S. / Wang, L. / Klussendorf, M. / Pusch, M. / Dutzler, R. / Stauber, T. | |||||||||
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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 | 29tc.cif.gz | 409.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb29tc.ent.gz | 318.5 KB | Display | PDB format |
| PDBx/mmJSON format | 29tc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/9t/29tc ftp://data.pdbj.org/pub/pdb/validation_reports/9t/29tc | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 57359MC ![]() 9t33C ![]() 9t34C ![]() 9t35C 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: 94408.516 Da / Num. of mol.: 6 / Mutation: I2C,L402W Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LRRC8A, KIAA1437, LRRC8, SWELL1, UNQ221/PRO247 / Production host: Homo sapiens (human) / References: UniProt: Q8IWT6Has 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: Volume-regulated anion channel subunit LRRC8A / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 8.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE-PROPANE |
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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: 2600 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 1.6 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.54 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 186012 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.54 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
Switzerland, 1items
Citation







PDBj







FIELD EMISSION GUN