9nr9

The structure of GluA1/A4 LBD-TMD with 2 TARPs

Method: ELECTRON MICROSCOPY Dmax: 142.6 Å Quality: GOOD

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

Voltage-dependent calcium channel gamma-2 subunit

OrganismNot specified

UniProt Q71RJ2

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 5–208 Chain H; UniProt 5–208 Not recorded Glutamate receptor 1 × 2 (P19490) Isoform 2 of Glutamate receptor 4 × 2 (P19493) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.22 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–204; UniProt 5–208 Author chain H; PDBConstruct 1–204; UniProt 5–208

Glutamate receptor 1

OrganismNot specified

UniProt P19490

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 407–833 Chain C; UniProt 407–833 Not recorded Voltage-dependent calcium channel gamma-2 subunit × 2 (Q71RJ2) Isoform 2 of Glutamate receptor 4 × 2 (P19493) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.22 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.

32 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–427; UniProt 407–833 Author chain C; PDBConstruct 1–427; UniProt 407–833

Isoform 2 of Glutamate receptor 4

OrganismNot specified

UniProt P19493

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 417–840 Chain D; UniProt 417–840 Not recorded Voltage-dependent calcium channel gamma-2 subunit × 2 (Q71RJ2) Glutamate receptor 1 × 2 (P19490) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.22 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.

25 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA4_RAT
Isoform P19493-2
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–424; UniProt 417–840 Author chain D; PDBConstruct 1–424; UniProt 417–840

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 9nr9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nr9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9nr9
Deposition date deposition_date2025-03-14
Structure title titleThe structure of GluA1/A4 LBD-TMD with 2 TARPs
Keywords keywordsiGluR, CP-AMPA receptors, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.86
Radius of gyration Rg (electron density) rg_electron43.66
Forward intensity I(0) i0516421000.00
Molecular weight molecular_weight194060.0 kDa
Excluded volume excluded_volume245560 ų
Envelope volume envelope_volume367770 ų
Hydration-shell volume shell_volume70445 ų
Envelope diameter envelope_diameter137.9
Shell Rg shell_rg48.46
Envelope Rg envelope_rg42.53
Shape Rg shape_rg43.65
Total Rg total_rg43.93
Total atoms total_atoms13679
Residues n_residues1865
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 dmax142.6
Rg (real space) rg_real43.69
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real5.1640e+08
I(0) uncertainty (real space) i0_real_error8.1110e+06
Rg (reciprocal space) rg_reciprocal43.86
I(0) (reciprocal space) i0_reciprocal516500000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.4
Skewness Skewness skewness0.135
Kurtosis Kurtosis kurtosis-0.579
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha102300000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)