+Open data
-Basic information
Entry | Database: PDB / ID: 7w6t | |||||||||||||||
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Title | CryoEM structure of human KChIP1-Kv4.3-DPP6 complex | |||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Kv channel-interacting protein 1 Potassium voltage-gated channel Dipeptidyl aminopeptidase-like protein 6 | |||||||||||||||
Function / homology | Function and homology information ventricular cardiac muscle cell membrane repolarization / Kv4.3-KChIP1 channel complex / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / membrane repolarization during ventricular cardiac muscle cell action potential / membrane repolarization during cardiac muscle cell action potential / potassium ion export across plasma membrane / membrane repolarization / Voltage gated Potassium channels / regulation of potassium ion transmembrane transport ...ventricular cardiac muscle cell membrane repolarization / Kv4.3-KChIP1 channel complex / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / membrane repolarization during ventricular cardiac muscle cell action potential / membrane repolarization during cardiac muscle cell action potential / potassium ion export across plasma membrane / membrane repolarization / Voltage gated Potassium channels / regulation of potassium ion transmembrane transport / postsynaptic specialization membrane / regulation of heart contraction / action potential / regulation of heart rate by cardiac conduction / voltage-gated potassium channel activity / potassium channel activity / potassium channel regulator activity / voltage-gated potassium channel complex / GABA-ergic synapse / muscle contraction / serine-type peptidase activity / protein homooligomerization / potassium ion transport / sarcolemma / cytoplasmic side of plasma membrane / chemical synaptic transmission / postsynaptic membrane / transmembrane transporter binding / dendritic spine / neuronal cell body / dendrite / calcium ion binding / synapse / proteolysis / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | Homo sapiens (human) Mus musculus (house mouse) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.85 Å | |||||||||||||||
Authors | Ma, D.M. / Guo, J.T. | |||||||||||||||
Funding support | China, 4items
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Citation | Journal: Cell Res / Year: 2022 Title: Structural basis for the gating modulation of Kv4.3 by auxiliary subunits. Authors: Demin Ma / Cheng Zhao / Xiaochen Wang / Xiaoxiao Li / Yi Zha / Yan Zhang / Guosheng Fu / Ping Liang / Jiangtao Guo / Dongwu Lai / | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7w6t.cif.gz | 710.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7w6t.ent.gz | 576.7 KB | Display | PDB format |
PDBx/mmJSON format | 7w6t.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7w6t_validation.pdf.gz | 908.2 KB | Display | wwPDB validaton report |
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Full document | 7w6t_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | 7w6t_validation.xml.gz | 119.6 KB | Display | |
Data in CIF | 7w6t_validation.cif.gz | 182.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w6/7w6t ftp://data.pdbj.org/pub/pdb/validation_reports/w6/7w6t | HTTPS FTP |
-Related structure data
Related structure data | 32335MC 7w3yC 7w6nC 7w6sC 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: 26935.469 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCNIP1, KCHIP1, VABP / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9NZI2 #2: Protein | Mass: 71472.781 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCND3 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9UK17 #3: Protein | Mass: 98874.242 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Dpp6 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: E9PWX1 |
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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: Complex of voltage-gated potassium channel Kv4.3 with auxiliary subunits KChIP1 and DPP6 Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | ||||||||||||
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Source (natural) |
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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: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: -1300 nm / Nominal defocus min: -1100 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
Image recording | Average exposure time: 2.8 sec. / Electron dose: 65 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: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.85 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 263176 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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