+Open data
-Basic information
Entry | Database: PDB / ID: 8x90 | ||||||
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Title | P/Q type calcium channel | ||||||
Components | (Voltage-dependent ...) x 3 | ||||||
Keywords | MEMBRANE PROTEIN / voltage-gated calcium channel | ||||||
Function / homology | Function and homology information regulation of membrane repolarization during action potential / Presynaptic depolarization and calcium channel opening / positive regulation of high voltage-gated calcium channel activity / calcium ion transmembrane transport via high voltage-gated calcium channel / membrane depolarization during bundle of His cell action potential / high voltage-gated calcium channel activity / L-type voltage-gated calcium channel complex / cardiac muscle cell action potential involved in contraction / NCAM1 interactions / regulation of ventricular cardiac muscle cell membrane repolarization ...regulation of membrane repolarization during action potential / Presynaptic depolarization and calcium channel opening / positive regulation of high voltage-gated calcium channel activity / calcium ion transmembrane transport via high voltage-gated calcium channel / membrane depolarization during bundle of His cell action potential / high voltage-gated calcium channel activity / L-type voltage-gated calcium channel complex / cardiac muscle cell action potential involved in contraction / NCAM1 interactions / regulation of ventricular cardiac muscle cell membrane repolarization / calcium ion transport into cytosol / syntaxin binding / regulation of calcium ion transmembrane transport via high voltage-gated calcium channel / voltage-gated calcium channel complex / neuromuscular junction development / calcium ion import across plasma membrane / neuronal dense core vesicle / regulation of heart rate by cardiac conduction / response to amyloid-beta / regulation of calcium ion transport / calcium channel regulator activity / voltage-gated calcium channel activity / sarcoplasmic reticulum / protein localization to plasma membrane / cell projection / Regulation of insulin secretion / calcium ion transmembrane transport / modulation of chemical synaptic transmission / Adrenaline,noradrenaline inhibits insulin secretion / cellular response to amyloid-beta / calcium ion transport / T cell receptor signaling pathway / amyloid-beta binding / positive regulation of cytosolic calcium ion concentration / chemical synaptic transmission / neuronal cell body / synapse / extracellular exosome / membrane / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.95 Å | ||||||
Authors | Yan, N. / Li, Z. / Cong, Y. / Wu, T. / Wang, T. | ||||||
Funding support | China, 1items
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Citation | Journal: Cell Res / Year: 2024 Title: Structural basis for different ω-agatoxin IVA sensitivities of the P-type and Q-type Ca2.1 channels. Authors: Zhangqiang Li / Ye Cong / Tong Wu / Tongtong Wang / Xinyao Lou / Xinyu Yang / Nieng Yan / | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8x90.cif.gz | 537.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8x90.ent.gz | 412 KB | Display | PDB format |
PDBx/mmJSON format | 8x90.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8x90_validation.pdf.gz | 2.2 MB | Display | wwPDB validaton report |
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Full document | 8x90_full_validation.pdf.gz | 2.2 MB | Display | |
Data in XML | 8x90_validation.xml.gz | 86.2 KB | Display | |
Data in CIF | 8x90_validation.cif.gz | 125.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x9/8x90 ftp://data.pdbj.org/pub/pdb/validation_reports/x9/8x90 | HTTPS FTP |
-Related structure data
Related structure data | 38158MC 8x91C 8x93C 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
-Voltage-dependent ... , 3 types, 3 molecules ABC
#1: Protein | Mass: 287534.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CACNA1A, CACH4, CACN3, CACNL1A4 / Production host: Homo sapiens (human) / References: UniProt: O00555 |
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#2: Protein | Mass: 126316.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CACNA2D1, CACNL2A, CCHL2A, MHS3 / Production host: Homo sapiens (human) / References: UniProt: P54289 |
#3: Protein | Mass: 56231.570 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CACNB3, CACNLB3 / Production host: Homo sapiens (human) / References: UniProt: P54284 |
-Sugars , 4 types, 7 molecules
#4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||
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#5: Polysaccharide | Source method: isolated from a genetically manipulated source #6: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #11: Sugar | |
-Non-polymers , 6 types, 14 molecules
#7: Chemical | ChemComp-PS1 / | ||||||||
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#8: Chemical | ChemComp-CLR / #9: Chemical | ChemComp-PT5 / [( | #10: Chemical | #12: Chemical | #13: Chemical | |
-Details
Has ligand of interest | N |
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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: Voltage-gated P/Q type calcium channel / Type: COMPLEX / Entity ID: #1-#3 / 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: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1300 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software | Name: PHENIX / Version: 1.19.2_4158: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.95 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 118997 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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