+Open data
-Basic information
Entry | Database: PDB / ID: 7xf5 | ||||||
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Title | Full length human CLC-2 channel in apo state | ||||||
Components | Chloride channel protein 2 | ||||||
Keywords | MEMBRANE PROTEIN / homo-dimer | ||||||
Function / homology | Function and homology information regulation of aldosterone biosynthetic process / cell differentiation involved in salivary gland development / astrocyte end-foot / acinar cell differentiation / voltage-gated chloride channel activity / dendritic spine membrane / chloride transport / phagocytosis, engulfment / positive regulation of oligodendrocyte differentiation / chloride channel complex ...regulation of aldosterone biosynthetic process / cell differentiation involved in salivary gland development / astrocyte end-foot / acinar cell differentiation / voltage-gated chloride channel activity / dendritic spine membrane / chloride transport / phagocytosis, engulfment / positive regulation of oligodendrocyte differentiation / chloride channel complex / lung development / Stimuli-sensing channels / myelin sheath / retina development in camera-type eye / basolateral plasma membrane / perikaryon / postsynaptic membrane / axon / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||
Authors | Wang, L. | ||||||
Funding support | China, 1items
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Citation | Journal: Nat Commun / Year: 2023 Title: Cryo-EM structures of ClC-2 chloride channel reveal the blocking mechanism of its specific inhibitor AK-42 Authors: Ma, T. / Wang, L. / Chai, A. / Liu, C. / Cui, W. / Yuan, S. / Wing Ngor Au, S. / Sun, L. / Zhang, X. / Zhang, Z. / Lu, J. / Gao, Y. / Wang, P. / Li, Z. / Liang, Y. / Vogel, H. / Wang, Y.T. / ...Authors: Ma, T. / Wang, L. / Chai, A. / Liu, C. / Cui, W. / Yuan, S. / Wing Ngor Au, S. / Sun, L. / Zhang, X. / Zhang, Z. / Lu, J. / Gao, Y. / Wang, P. / Li, Z. / Liang, Y. / Vogel, H. / Wang, Y.T. / Wang, D. / Yan, K. / Zhang, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7xf5.cif.gz | 227 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7xf5.ent.gz | 176.8 KB | Display | PDB format |
PDBx/mmJSON format | 7xf5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7xf5_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 7xf5_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 7xf5_validation.xml.gz | 46.7 KB | Display | |
Data in CIF | 7xf5_validation.cif.gz | 69.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xf/7xf5 ftp://data.pdbj.org/pub/pdb/validation_reports/xf/7xf5 | HTTPS FTP |
-Related structure data
Related structure data | 33169MC 7xjaC 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
#1: Protein | Mass: 98642.352 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CLCN2 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P51788 |
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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 |
-Sample preparation
Component | Name: Full length human CLC-2 homo dimer / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Value: 180 kDa/nm / Experimental value: YES |
Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Homo sapiens (human) / Cell: HEK293 |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Instrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 300 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.16_3549: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: NONE | ||||||||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 43510 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT | ||||||||||||||||||||||||
Refine LS restraints |
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