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- PDB-5vhz: GluA2-2xGSG1L bound to L-Quisqualate -

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Database: PDB / ID: 5vhz
TitleGluA2-2xGSG1L bound to L-Quisqualate
DescriptorGlutamate receptor 2,Germ cell-specific gene 1-like protein
KeywordsTRANSPORT PROTEIN / Ion channel
Specimen sourceRattus norvegicus / mammal / Rat / ドブネズミ, どぶねずみ /
MethodElectron microscopy (8.4 Å resolution / Particle / Single particle)
AuthorsTwomey, E.C. / Yelshanskaya, M.V. / Grassucci, R.A. / Frank, J. / Sobolevsky, A.I.
CitationNeuron, 2017, 94, 569-580.e5

Neuron, 2017, 94, 569-580.e5 StrPapers
Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes.
Edward C Twomey / Maria V Yelshanskaya / Robert A Grassucci / Joachim Frank / Alexander I Sobolevsky

Validation Report
SummaryFull reportAbout validation report
DateDeposition: Apr 13, 2017 / Release: May 3, 2017
RevisionDateData content typeGroupProviderType
1.0May 3, 2017Structure modelrepositoryInitial release
1.1May 17, 2017Structure modelDatabase references

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Deposited unit
A: Glutamate receptor 2,Germ cell-specific gene 1-like protein
B: Glutamate receptor 2,Germ cell-specific gene 1-like protein
C: Glutamate receptor 2,Germ cell-specific gene 1-like protein
D: Glutamate receptor 2,Germ cell-specific gene 1-like protein
E: Glutamate receptor 2,Germ cell-specific gene 1-like protein
F: Glutamate receptor 2,Germ cell-specific gene 1-like protein
hetero molecules

Theoretical massNumber of molelcules
Total (without water)705,58410

TypeNameSymmetry operationNumber
identity operation1_5551
Buried area (Å2)30010
ΔGint (kcal/M)-288
Surface area (Å2)159720


#1: Polypeptide(L)
Glutamate receptor 2,Germ cell-specific gene 1-like protein / GluR-2 / AMPA-selective glutamate receptor 2 / GluR-B / GluR-K2 / Glutamate receptor ionotropic / AMPA 2 / GluA2 / GSG1-like protein

Mass: 117471.211 Da / Num. of mol.: 6
Source: (gene. exp.) Rattus norvegicus / mammal / ドブネズミ, どぶねずみ /
References: UniProt: P19491, UniProt: D3ZK93

Cellular component

Molecular function

Biological process

#2: Chemical

Mass: 189.126 Da / Num. of mol.: 4 / Formula: C5H7N3O5

Experimental details


EM experimentAggregation state: PARTICLE / Reconstruction method: SINGLE PARTICLE

Sample preparation

ComponentName: GluA2-2xGSG1L bound to L-Quisqualate cryo-EM density / Type: COMPLEX / Entity ID: 1, 2, 3 / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Rattus norvegicus
Source (recombinant)Organism: Rattus norvegicus
Buffer solutionpH: 8
SpecimenConc.: 5 mg/ml / Details: GluA2-2xGSG1L bound to L-Quisqualate / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: Gold-gold grids, hydrogen and oxygen glow discharge (20s, 10 watts, 6.4 sccm H2, 27.5 sccm O2)
Grid material: GOLD / Grid mesh size: 200 / Grid type: C-flat 1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 295 kelvins

Electron microscopy imaging

Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company
MicroscopyMicroscope model: FEI POLARA 300
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 67 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)


SymmetryPoint symmetry: C2
3D reconstructionResolution: 8.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 51130 / Symmetry type: POINT

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