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Open data
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Basic information
| Entry | Database: PDB / ID: 8vav | ||||||||||||||||||||||||||||||
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| Title | Human Slo1 - human LRRC26 in presence of EDTA - GR masked | ||||||||||||||||||||||||||||||
Components |
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Keywords | TRANSPORT PROTEIN / Slo1 / BK / maxiK / potassium channel / voltage sensor / VSD / resting state / LRRC26 / Gamma1 | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationpositive regulation of voltage-gated potassium channel activity / Acetylcholine inhibits contraction of outer hair cells / micturition / large conductance calcium-activated potassium channel activity / Ca2+ activated K+ channels / potassium channel activator activity / calcium-activated potassium channel activity / negative regulation of cell volume / smooth muscle contraction involved in micturition / response to carbon monoxide ...positive regulation of voltage-gated potassium channel activity / Acetylcholine inhibits contraction of outer hair cells / micturition / large conductance calcium-activated potassium channel activity / Ca2+ activated K+ channels / potassium channel activator activity / calcium-activated potassium channel activity / negative regulation of cell volume / smooth muscle contraction involved in micturition / response to carbon monoxide / response to osmotic stress / Sensory processing of sound by inner hair cells of the cochlea / cGMP effects / intracellular potassium ion homeostasis / voltage-gated potassium channel activity / potassium channel regulator activity / voltage-gated potassium channel complex / potassium ion transmembrane transport / regulation of membrane potential / response to calcium ion / caveola / potassium ion transport / vasodilation / actin binding / transmembrane transporter binding / postsynaptic membrane / cytoskeleton / response to hypoxia / apical plasma membrane / positive regulation of apoptotic process / extracellular exosome / metal ion binding / identical protein binding / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.13 Å | ||||||||||||||||||||||||||||||
Authors | Pal, K. / Kallure, G.S. / Chowdhury, S. | ||||||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Human Slo1 - human LRRC26 in presence of EDTA - GR masked Authors: Pal, K. / Kallure, G. / Chowdhury, 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 | 8vav.cif.gz | 531.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8vav.ent.gz | 401.2 KB | Display | PDB format |
| PDBx/mmJSON format | 8vav.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/va/8vav ftp://data.pdbj.org/pub/pdb/validation_reports/va/8vav | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 43106MC 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
-Protein , 2 types, 8 molecules ABCDEFGH
| #1: Protein | Mass: 119988.062 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCNMA1, KCNMA, SLO / Production host: Homo sapiens (human) / References: UniProt: Q12791#2: Protein | Mass: 35893.773 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LRRC26 / Production host: Homo sapiens (human) / References: UniProt: Q2I0M4 |
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-Sugars , 1 types, 4 molecules 
| #7: Sugar | ChemComp-NAG / |
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-Non-polymers , 4 types, 60 molecules 






| #3: Chemical | ChemComp-POV / ( #4: Chemical | ChemComp-K / #5: Chemical | ChemComp-AJP / #6: Chemical | ChemComp-CLR / |
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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: Hetero-octameric complex of hSlo1 (BK) channel and hLRRC26 subunits Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 8 |
| 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: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1700 nm / Nominal defocus min: 900 nm |
| Image recording | Electron dose: 72 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.13 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 390830 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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Movie
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation
PDBj















FIELD EMISSION GUN