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Open data
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Basic information
Entry | Database: PDB / ID: 6kzp | ||||||||||||||||||
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Title | calcium channel-ligand | ||||||||||||||||||
![]() | Voltage-dependent T-type calcium channel subunit alpha-1G,Voltage-dependent T-type calcium channel subunit alpha-1G | ||||||||||||||||||
![]() | MEMBRANE PROTEIN / channel / blocker | ||||||||||||||||||
Function / homology | ![]() SA node cell to atrial cardiac muscle cell signaling / AV node cell to bundle of His cell signaling / voltage-gated calcium channel activity involved SA node cell action potential / sinoatrial node development / low voltage-gated calcium channel activity / voltage-gated calcium channel activity involved in AV node cell action potential / AV node cell action potential / SA node cell action potential / membrane depolarization during SA node cell action potential / response to nickel cation ...SA node cell to atrial cardiac muscle cell signaling / AV node cell to bundle of His cell signaling / voltage-gated calcium channel activity involved SA node cell action potential / sinoatrial node development / low voltage-gated calcium channel activity / voltage-gated calcium channel activity involved in AV node cell action potential / AV node cell action potential / SA node cell action potential / membrane depolarization during SA node cell action potential / response to nickel cation / membrane depolarization during AV node cell action potential / positive regulation of calcium ion-dependent exocytosis / regulation of atrial cardiac muscle cell membrane depolarization / cardiac muscle cell action potential involved in contraction / calcium ion import / NCAM1 interactions / voltage-gated sodium channel complex / membrane depolarization during action potential / regulation of monoatomic ion transmembrane transport / voltage-gated calcium channel complex / voltage-gated sodium channel activity / regulation of heart rate by cardiac conduction / Smooth Muscle Contraction / neuronal action potential / regulation of membrane potential / calcium ion transmembrane transport / scaffold protein binding / chemical synaptic transmission / neuron projection / synapse / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||||||||
![]() | Yan, N. | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structures of apo and antagonist-bound human Ca3.1. Authors: Yanyu Zhao / Gaoxingyu Huang / Qiurong Wu / Kun Wu / Ruiqi Li / Jianlin Lei / Xiaojing Pan / Nieng Yan / ![]() ![]() Abstract: Among the ten subtypes of mammalian voltage-gated calcium (Ca) channels, Ca3.1-Ca3.3 constitute the T-type, or the low-voltage-activated, subfamily, the abnormal activities of which are associated ...Among the ten subtypes of mammalian voltage-gated calcium (Ca) channels, Ca3.1-Ca3.3 constitute the T-type, or the low-voltage-activated, subfamily, the abnormal activities of which are associated with epilepsy, psychiatric disorders and pain. Here we report the cryo-electron microscopy structures of human Ca3.1 alone and in complex with a highly Ca3-selective blocker, Z944, at resolutions of 3.3 Å and 3.1 Å, respectively. The arch-shaped Z944 molecule reclines in the central cavity of the pore domain, with the wide end inserting into the fenestration on the interface between repeats II and III, and the narrow end hanging above the intracellular gate like a plug. The structures provide the framework for comparative investigation of the distinct channel properties of different Ca subfamilies. | ||||||||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 222.6 KB | Display | ![]() |
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PDB format | ![]() | 164 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 40 KB | Display | |
Data in CIF | ![]() | 57.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 0792MC ![]() 0791C ![]() 6kzoC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Protein / Sugars , 2 types, 5 molecules A![](data/chem/img/NAG.gif)
![](data/chem/img/NAG.gif)
#1: Protein | Mass: 238874.984 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#3: Sugar | ChemComp-NAG / |
-Non-polymers , 4 types, 14 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/DZR.gif)
![](data/chem/img/3PE.gif)
![](data/chem/img/Y01.gif)
![](data/chem/img/DZR.gif)
![](data/chem/img/3PE.gif)
![](data/chem/img/Y01.gif)
#2: Chemical | #4: Chemical | ChemComp-DZR / ~{ | #5: Chemical | ChemComp-3PE / #6: Chemical | |
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-Details
Has ligand of interest | Y |
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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 |
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Sample preparation
Component | Name: membrane protein-ligand / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 48 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING ONLY |
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3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 138449 / Symmetry type: POINT |