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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Human BEST1 bound to GABA in an open state | |||||||||
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![]() | bestrophin / ion channel / GABA / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() membrane microdomain / bicarbonate channel activity / transepithelial chloride transport / gamma-aminobutyric acid secretion, neurotransmission / detection of light stimulus involved in visual perception / intracellularly calcium-gated chloride channel activity / ligand-gated channel activity / bicarbonate transmembrane transporter activity / glutamate secretion / chloride transport ...membrane microdomain / bicarbonate channel activity / transepithelial chloride transport / gamma-aminobutyric acid secretion, neurotransmission / detection of light stimulus involved in visual perception / intracellularly calcium-gated chloride channel activity / ligand-gated channel activity / bicarbonate transmembrane transporter activity / glutamate secretion / chloride transport / chloride channel activity / protein complex oligomerization / regulation of calcium ion transport / chloride channel complex / visual perception / basal plasma membrane / regulation of synaptic plasticity / Stimuli-sensing channels / presynapse / monoatomic ion transmembrane transport / basolateral plasma membrane / identical protein binding / membrane / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.45 Å | |||||||||
![]() | Pant S / Long SB | |||||||||
Funding support | ![]()
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![]() | ![]() Title: The pentameric chloride channel BEST1 is activated by extracellular GABA Authors: Pant S / Tam SW / Long SB | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 263.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.3 KB 15.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.8 KB | Display | ![]() |
Images | ![]() | 82.1 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 475.8 MB 475.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 840 KB | Display | ![]() |
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Full document | ![]() | 839.5 KB | Display | |
Data in XML | ![]() | 26.6 KB | Display | |
Data in CIF | ![]() | 34.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9egmMC ![]() 9efzC ![]() 9egqC ![]() 9egsC ![]() 9egtC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.725 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_47991_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_47991_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Human BEST1 bound to GABA in an open state
Entire | Name: Human BEST1 bound to GABA in an open state |
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Components |
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-Supramolecule #1: Human BEST1 bound to GABA in an open state
Supramolecule | Name: Human BEST1 bound to GABA in an open state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 237 kDa/nm |
-Macromolecule #1: Bestrophin-1
Macromolecule | Name: Bestrophin-1 / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 47.416449 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: TITYTSQVAN ARLGSFSRLL LCWRGSIYKL LYGEFLIFLL CYYIIRFIYR LALTEEQQLM FEKLTLYCDS YIQLIPISFV LGFYVTLVV TRWWNQYENL PWPDRLMSLV SGFVEGKDEQ GRLLRRTLIR YANLGNVLIL RSVSTAVYKR FPSAQHLVQA G FMTPAEHK ...String: TITYTSQVAN ARLGSFSRLL LCWRGSIYKL LYGEFLIFLL CYYIIRFIYR LALTEEQQLM FEKLTLYCDS YIQLIPISFV LGFYVTLVV TRWWNQYENL PWPDRLMSLV SGFVEGKDEQ GRLLRRTLIR YANLGNVLIL RSVSTAVYKR FPSAQHLVQA G FMTPAEHK QLEKLSLPHN MFWVPWVWFA NLSMKAWLGG RIRDPILLQS LLNEMNTLRT QCGHLYAYDW ISIPLVYTQV VT VAVYSFF LTCLVGRQFL NPAKAYPGHE LDLVVPVFTF LQFFFYVGWL KVAEQLINPF GEDDDDFETN WIVDRNLQVS LLA VDEMHQ DLPRMEPDMY WNKPEPQPPY TAASAQFRRA SFMGSTFNIS LNKEEMEFQP NQEDEEDAHA GIIGRFLGLQ SSNS LEVLF Q UniProtKB: Bestrophin-1 |
-Macromolecule #2: CHLORIDE ION
Macromolecule | Name: CHLORIDE ION / type: ligand / ID: 2 / Number of copies: 5 / Formula: CL |
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Molecular weight | Theoretical: 35.453 Da |
-Macromolecule #3: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 5 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Macromolecule #4: GAMMA-AMINO-BUTANOIC ACID
Macromolecule | Name: GAMMA-AMINO-BUTANOIC ACID / type: ligand / ID: 4 / Number of copies: 5 / Formula: ABU |
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Molecular weight | Theoretical: 103.12 Da |
Chemical component information | ![]() ChemComp-ABU: |
-Macromolecule #5: water
Macromolecule | Name: water / type: ligand / ID: 5 / Number of copies: 330 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.6 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.3 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |