+Open data
-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 information positive regulation of voltage-gated potassium channel activity / Acetylcholine inhibits contraction of outer hair cells / micturition / Ca2+ activated K+ channels / large conductance calcium-activated potassium channel activity / response to carbon monoxide / calcium-activated potassium channel activity / potassium channel activator activity / negative regulation of cell volume / smooth muscle contraction involved in micturition ...positive regulation of voltage-gated potassium channel activity / Acetylcholine inhibits contraction of outer hair cells / micturition / Ca2+ activated K+ channels / large conductance calcium-activated potassium channel activity / response to carbon monoxide / calcium-activated potassium channel activity / potassium channel activator activity / negative regulation of cell volume / smooth muscle contraction involved in micturition / intracellular potassium ion homeostasis / Sensory processing of sound by inner hair cells of the cochlea / response to osmotic stress / cGMP effects / voltage-gated potassium channel activity / potassium channel regulator activity / voltage-gated potassium channel complex / potassium ion transmembrane transport / regulation of membrane potential / potassium ion transport / caveola / response to calcium ion / vasodilation / actin binding / postsynaptic membrane / transmembrane transporter binding / cytoskeleton / response to hypoxia / positive regulation of apoptotic process / apical plasma membrane / extracellular exosome / identical protein binding / membrane / metal ion binding / 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 Published Title: Human Slo1 - human LRRC26 in presence of EDTA - GR masked Authors: Pal, K. / Kallure, G. / Chowdhury, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8vav.cif.gz | 531.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8vav.ent.gz | 401.1 KB | Display | PDB format |
PDBx/mmJSON format | 8vav.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8vav_validation.pdf.gz | 3.3 MB | Display | wwPDB validaton report |
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Full document | 8vav_full_validation.pdf.gz | 3.4 MB | Display | |
Data in XML | 8vav_validation.xml.gz | 73.7 KB | Display | |
Data in CIF | 8vav_validation.cif.gz | 100.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/va/8vav ftp://data.pdbj.org/pub/pdb/validation_reports/va/8vav | HTTPS FTP |
-Related structure data
Related structure data | 43106MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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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 |
-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 |
-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) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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3D reconstruction | Resolution: 3.13 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 390830 / Symmetry type: POINT | ||||||||||||||||||||||||
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