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- EMDB-20377: CryoEM structure of zebra fish alpha-1 glycine receptor bound wit... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-20377 | |||||||||
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Title | CryoEM structure of zebra fish alpha-1 glycine receptor bound with GABA in nanodisc, closed state | |||||||||
![]() | zebra fish alpha-1 glycine receptor bound with GABA in nanodisc, closed state | |||||||||
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![]() | glycine receptor / nanodisc / CryoEM / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() Neurotransmitter receptors and postsynaptic signal transmission / extracellularly glycine-gated ion channel activity / extracellularly glycine-gated chloride channel activity / transmitter-gated monoatomic ion channel activity / regulation of neuron differentiation / ligand-gated monoatomic ion channel activity / glycine binding / cellular response to zinc ion / cellular response to ethanol / response to amino acid ...Neurotransmitter receptors and postsynaptic signal transmission / extracellularly glycine-gated ion channel activity / extracellularly glycine-gated chloride channel activity / transmitter-gated monoatomic ion channel activity / regulation of neuron differentiation / ligand-gated monoatomic ion channel activity / glycine binding / cellular response to zinc ion / cellular response to ethanol / response to amino acid / chloride channel complex / monoatomic ion transport / chloride transmembrane transport / central nervous system development / cellular response to amino acid stimulus / transmembrane signaling receptor activity / perikaryon / postsynaptic membrane / dendrite / zinc ion binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Yu J / Zhu H | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Mechanism of gating and partial agonist action in the glycine receptor. Authors: Yu J / Zhu H / Lape R / Greiner T / Du J / Lu W / Sivilotti L / Gouaux E | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
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Downloads & links
-EMDB archive
Map data | ![]() | 165.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 10.2 KB 10.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.8 KB | Display | ![]() |
Images | ![]() | 73.8 KB | ||
Filedesc metadata | ![]() | 5.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 575.9 KB | Display | ![]() |
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Full document | ![]() | 575.4 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 18.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6plvMC ![]() 6ploC ![]() 6plpC ![]() 6plqC ![]() 6plrC ![]() 6plsC ![]() 6pltC ![]() 6pluC ![]() 6plwC ![]() 6plxC ![]() 6plyC ![]() 6plzC ![]() 6pm0C ![]() 6pm1C ![]() 6pm2C ![]() 6pm3C ![]() 6pm4C ![]() 6pm5C ![]() 6pm6C ![]() 6pxdC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | zebra fish alpha-1 glycine receptor bound with GABA in nanodisc, closed state | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.91 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : glycine receptor in complex with GABA
Entire | Name: glycine receptor in complex with GABA |
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Components |
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-Supramolecule #1: glycine receptor in complex with GABA
Supramolecule | Name: glycine receptor in complex with GABA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 250 KDa |
-Macromolecule #1: Glycine receptor subunit alphaZ1
Macromolecule | Name: Glycine receptor subunit alphaZ1 / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 52.537598 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MFALGIYLWE TIVFFSLAAS QQAAARKAAS PMPPSEFLDK LMGKVSGYDA RIRPNFKGPP VNVTCNIFIN SFGSIAETTM DYRVNIFLR QQWNDPRLAY SEYPDDSLDL DPSMLDSIWK PDLFFANEKG ANFHEVTTDN KLLRISKNGN VLYSIRITLV L ACPMDLKN ...String: MFALGIYLWE TIVFFSLAAS QQAAARKAAS PMPPSEFLDK LMGKVSGYDA RIRPNFKGPP VNVTCNIFIN SFGSIAETTM DYRVNIFLR QQWNDPRLAY SEYPDDSLDL DPSMLDSIWK PDLFFANEKG ANFHEVTTDN KLLRISKNGN VLYSIRITLV L ACPMDLKN FPMDVQTCIM QLESFGYTMN DLIFEWDEKG AVQVADGLTL PQFILKEEKD LRYCTKHYNT GKFTCIEARF HL ERQMGYY LIQMYIPSLL IVILSWVSFW INMDAAPARV GLGITTVLTM TTQSSGSRAS LPKVSYVKAI DIWMAVCLLF VFS ALLEYA AVNFIARQHK ELLRFQRRRR HLKEDEAGDG RFSFAAYGMG PACLQAKDGM AIKGNNNNAP TSTNPPEKTV EEMR KLFIS RAKRIDTVSR VAFPLVFLIF NIFYWITYKI IRSEDIHKQL VPRGSHHHHH HHH UniProtKB: Glycine receptor subunit alphaZ1 |
-Macromolecule #3: UNKNOWN LIGAND
Macromolecule | Name: UNKNOWN LIGAND / type: ligand / ID: 3 / Number of copies: 60 / Formula: UNL |
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Molecular weight | Theoretical: 142.282 Da |
Chemical component information | ![]()
ChemComp-UNL: |
-Macromolecule #4: GAMMA-AMINO-BUTANOIC ACID
Macromolecule | Name: GAMMA-AMINO-BUTANOIC ACID / type: ligand / ID: 4 / Number of copies: 5 / Formula: ABU |
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Molecular weight | Theoretical: 103.12 Da |
Chemical component information | ![]() ChemComp-ABU: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 61.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Applied symmetry - Point group: C5 (5 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 38383 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |