9zkq

The LBD-TMD structure of native mouse AMPAR with 3 TARPs 1 CNIH

Method: ELECTRON MICROSCOPY Dmax: 145.4 Å Quality: GOOD

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

Glutamate receptor 1

OrganismNot specified

UniProt P23818

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 A; UniProt 408–907 Chain C; UniProt 408–907 Not recorded Glutamate receptor 2 × 2 (C9K0Z0) Protein cornichon homolog 2 × 1 (O35089) Voltage-dependent calcium channel gamma-2 subunit × 1 (O88602) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) PLM PALMITIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–500; UniProt 408–907 Author chain C; PDBConstruct 1–500; UniProt 408–907

Glutamate receptor 2

OrganismNot specified

UniProt C9K0Z0

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 417–883 Chain D; UniProt 417–883 Not recorded Glutamate receptor 1 × 2 (P23818) Protein cornichon homolog 2 × 1 (O35089) Voltage-dependent calcium channel gamma-2 subunit × 1 (O88602) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) PLM PALMITIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C9K0Z0_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–467; UniProt 417–883 Author chain D; PDBConstruct 1–467; UniProt 417–883

Protein cornichon homolog 2

OrganismNot specified

UniProt O35089

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 E; UniProt 1–160 Not recorded Glutamate receptor 1 × 2 (P23818) Glutamate receptor 2 × 2 (C9K0Z0) Voltage-dependent calcium channel gamma-2 subunit × 1 (O88602) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) PLM PALMITIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNIH2_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–160; UniProt 1–160

Voltage-dependent calcium channel gamma-2 subunit

OrganismNot specified

UniProt O88602

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 F; UniProt 1–323 Not recorded Glutamate receptor 1 × 2 (P23818) Glutamate receptor 2 × 2 (C9K0Z0) Protein cornichon homolog 2 × 1 (O35089) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) PLM PALMITIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

39 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG2_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–323; UniProt 1–323

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 1–423 Chain H; UniProt 1–423 Not recorded Glutamate receptor 1 × 2 (P23818) Glutamate receptor 2 × 2 (C9K0Z0) Protein cornichon homolog 2 × 1 (O35089) Voltage-dependent calcium channel gamma-2 subunit × 1 (O88602) PLM PALMITIC ACID × 10 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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 5
Chains and sequence ranges Author chain G; PDBConstruct 1–423; UniProt 1–423 Author chain H; PDBConstruct 1–423; UniProt 1–423

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 9zkq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zkq
Deposition date deposition_date2025-12-07
Structure title titleThe LBD-TMD structure of native mouse AMPAR with 3 TARPs 1 CNIH
Keywords keywordsiGluR, AMPA receptors, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.73
Radius of gyration Rg (electron density) rg_electron43.94
Forward intensity I(0) i0761436000.00
Molecular weight molecular_weight249640.0 kDa
Excluded volume excluded_volume321180 ų
Envelope volume envelope_volume442060 ų
Hydration-shell volume shell_volume81657 ų
Envelope diameter envelope_diameter150.1
Shell Rg shell_rg50.52
Envelope Rg envelope_rg43.21
Shape Rg shape_rg43.94
Total Rg total_rg44.25
Total atoms total_atoms17595
Residues n_residues2286
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 dmax145.4
Rg (real space) rg_real44.53
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real7.6140e+08
I(0) uncertainty (real space) i0_real_error1.1830e+07
Rg (reciprocal space) rg_reciprocal44.73
I(0) (reciprocal space) i0_reciprocal761600000.0000
Solution quality estimate total_estimate0.8896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.0
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha83940000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.907

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)