9z6w

The structure of TMD with 4 TARPs from all native AMPA receptor subtypes

Method: ELECTRON MICROSCOPY Dmax: 108.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Glutamate receptor 2

OrganismNot specified

UniProt P23819

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 532–568 Chain B; UniProt 590–651 Chain B; UniProt 805–841 Chain D; UniProt 532–568 Chain D; UniProt 590–651 Chain D; UniProt 805–841 Not recorded Mix of AMPAR subunit (GluA1, GluA2, GluA3 and GluA4) × 2 Mix of voltage-dependent calcium channel gamma subunits × 2 Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 C14 TETRADECANE × 18 OCT N-OCTANE × 2 XVD 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.99 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–37; UniProt 532–568 Author chain B; PDBConstruct 59–120; UniProt 590–651 Author chain B; PDBConstruct 274–310; UniProt 805–841 Author chain D; PDBConstruct 1–37; UniProt 532–568 Author chain D; PDBConstruct 59–120; UniProt 590–651 Author chain D; PDBConstruct 274–310; UniProt 805–841

Voltage-dependent calcium channel gamma-8 subunit

OrganismNot specified

UniProt Q8VHW2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 2–423 Chain H; UniProt 2–423 Not recorded Mix of AMPAR subunit (GluA1, GluA2, GluA3 and GluA4) × 2 Glutamate receptor 2 × 2 (P23819) Mix of voltage-dependent calcium channel gamma subunits × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 8 C14 TETRADECANE × 18 OCT N-OCTANE × 2 XVD 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.99 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG8_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–422; UniProt 2–423 Author chain H; PDBConstruct 1–422; UniProt 2–423

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9z6w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9z6w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9z6w
Deposition date deposition_date2025-11-14
Structure title titleThe structure of TMD with 4 TARPs from all native AMPA receptor subtypes
Keywords keywordsIonotropic glutamate receptor AMPA receptor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.16
Radius of gyration Rg (electron density) rg_electron32.78
Forward intensity I(0) i0179465000.00
Molecular weight molecular_weight122960.0 kDa
Excluded volume excluded_volume160260 ų
Envelope volume envelope_volume200110 ų
Hydration-shell volume shell_volume49760 ų
Envelope diameter envelope_diameter114.1
Shell Rg shell_rg40.60
Envelope Rg envelope_rg33.02
Shape Rg shape_rg32.76
Total Rg total_rg33.51
Total atoms total_atoms8704
Residues n_residues1144
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax108.0
Rg (real space) rg_real34.01
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.7950e+08
I(0) uncertainty (real space) i0_real_error2.9300e+06
Rg (reciprocal space) rg_reciprocal34.11
I(0) (reciprocal space) i0_reciprocal179500000.0000
Solution quality estimate total_estimate0.8895
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.158
Kurtosis Kurtosis kurtosis-0.351
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15950000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)