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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | CLC-ec1 at pH 4.5 100mM Cl Turn | |||||||||
![]() | CLC-ec1 100 mM Cl pH 4.5 TURN | |||||||||
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![]() | CLC / chloride transporter / MEMBRANE PROTEIN | |||||||||
Function / homology | Chloride channel, ClcA / Chloride channel, voltage gated / Chloride channel, core / Voltage gated chloride channel / voltage-gated chloride channel activity / antiporter activity / plasma membrane / H(+)/Cl(-) exchange transporter ClcA![]() | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.72 Å | |||||||||
![]() | Fortea E / Boudker O | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of common gate activation in CLC transporters Authors: Fortea E / Lee S / Argyros Y / Chadda R / Ciftci D / Huysmans G / Robertson JL / Boudker O / Accardi A | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 2.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.3 KB 9.3 KB | Display Display | ![]() |
Images | ![]() | 45 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 376.6 KB | Display | ![]() |
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Full document | ![]() | 376.2 KB | Display | |
Data in XML | ![]() | 5.7 KB | Display | |
Data in CIF | ![]() | 6.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7rp5MC ![]() 7n8pC ![]() 7n9wC ![]() 7rnxC ![]() 7ro0C ![]() 7rp6C ![]() 7rq7C ![]() 7rsbC 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
File | ![]() | ||||||||||||||||||||
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Annotation | CLC-ec1 100 mM Cl pH 4.5 TURN | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.048 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Structure of ecCLC at pH 4.5 in 100mM Cl
Entire | Name: Structure of ecCLC at pH 4.5 in 100mM Cl |
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Components |
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-Supramolecule #1: Structure of ecCLC at pH 4.5 in 100mM Cl
Supramolecule | Name: Structure of ecCLC at pH 4.5 in 100mM Cl / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 100 kDa/nm |
-Macromolecule #1: H(+)/Cl(-) exchange transporter ClcA
Macromolecule | Name: H(+)/Cl(-) exchange transporter ClcA / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 50.390402 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKTDTPSLET PQAARLRRRQ LIRQLLERDK TPLAILFMAA VVGTLVGLAA VAFDKGVAWL QNQRMGALVH TADNYPLLLT VAFLCSAVL AMFGYFLVRK YAPEAGGSGI PEIEGALEDQ RPVRWWRVLP VKFFGGLGTL GGGMVLGREG PTVQIGGNIG R MVLDIFRL ...String: MKTDTPSLET PQAARLRRRQ LIRQLLERDK TPLAILFMAA VVGTLVGLAA VAFDKGVAWL QNQRMGALVH TADNYPLLLT VAFLCSAVL AMFGYFLVRK YAPEAGGSGI PEIEGALEDQ RPVRWWRVLP VKFFGGLGTL GGGMVLGREG PTVQIGGNIG R MVLDIFRL KGDEARHTLL ATGAAAGLAA AFNAPLAGIL FIIEEMRPQF RYTLISIKAV FIGVIMSTIM YRIFNHEVAL ID VGKLSDA PLNTLWLYLI LGIIFGIFGP IFNKWVLGMQ DLLHRVHGGN ITKWVLMGGA IGGLCGLLGF VAPATSGGGF NLI PIATAG NFSMGMLVFI FVARVITTLL CFSSGAPGGI FAPMLALGTV LGTAFGMVAV ELFPQYHLEA GTFAIAGMGA LLAA SIRAP LTGIILVLEM TDNYQLILPM IITGLGATLL AQFTGGKPLY SAILARTLAK QEAEQLARSK AASASENT UniProtKB: H(+)/Cl(-) exchange transporter ClcA |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1.7 mg/mL |
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Buffer | pH: 4.5 |
Grid | Model: UltrAuFoil R1.2/1.3 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 294.15 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 72.61 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.72 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 59069 |
Initial angle assignment | Type: OTHER |
Final angle assignment | Type: OTHER |