9zks

The LBD-TMD structure of native mouse AMPAR with 2 TARPs 2 CNIHs and PRRT1/SynDIG4

Method: ELECTRON MICROSCOPY Dmax: 149.4 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 × 9 PDB declaration: nonameric(9) 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 × 2 (O35089) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) Proline-rich transmembrane protein 1 × 1 (O35449) PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 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 × 9 PDB declaration: nonameric(9) 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 × 2 (O35089) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) Proline-rich transmembrane protein 1 × 1 (O35449) PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain E; UniProt 1–160 Chain F; UniProt 1–160 Not recorded Glutamate receptor 1 × 2 (P23818) Glutamate receptor 2 × 2 (C9K0Z0) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) Proline-rich transmembrane protein 1 × 1 (O35449) PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 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 Author chain F; PDBConstruct 1–160; UniProt 1–160

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 × 9 PDB declaration: nonameric(9) 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 × 2 (O35089) Proline-rich transmembrane protein 1 × 1 (O35449) PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 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 4
Chains and sequence ranges Author chain G; PDBConstruct 1–423; UniProt 1–423 Author chain H; PDBConstruct 1–423; UniProt 1–423

Proline-rich transmembrane protein 1

OrganismNot specified

UniProt O35449

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain M; UniProt 1–306 Not recorded Glutamate receptor 1 × 2 (P23818) Glutamate receptor 2 × 2 (C9K0Z0) Protein cornichon homolog 2 × 2 (O35089) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 3 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRRT1_MOUSE
Isoform
PDB entities 5
Chains and sequence ranges Author chain M; PDBConstruct 1–306; UniProt 1–306

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 9zks

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zks
Deposition date deposition_date2025-12-07
Structure title titleThe LBD-TMD structure of native mouse AMPAR with 2 TARPs 2 CNIHs and PRRT1/SynDIG4
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_guinier45.64
Radius of gyration Rg (electron density) rg_electron44.77
Forward intensity I(0) i0713497000.00
Molecular weight molecular_weight240660.0 kDa
Excluded volume excluded_volume309120 ų
Envelope volume envelope_volume431030 ų
Hydration-shell volume shell_volume78772 ų
Envelope diameter envelope_diameter154.8
Shell Rg shell_rg50.22
Envelope Rg envelope_rg44.26
Shape Rg shape_rg44.78
Total Rg total_rg44.99
Total atoms total_atoms16983
Residues n_residues2267
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 dmax149.4
Rg (real space) rg_real45.48
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real7.1350e+08
I(0) uncertainty (real space) i0_real_error1.2670e+07
Rg (reciprocal space) rg_reciprocal45.64
I(0) (reciprocal space) i0_reciprocal713600000.0000
Solution quality estimate total_estimate0.8847
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.8
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha94600000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)