9rms

GluA4 in complex with TARP-2, Resting II state, structure of TMD/LBD domains

Method: ELECTRON MICROSCOPY Dmax: 145.9 Å Quality: GOOD

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

Isoform 2 of Glutamate receptor 4

Rattus norvegicus

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 21–902 Chain B; UniProt 21–902 Chain C; UniProt 21–902 Chain D; UniProt 21–902 Not recorded Voltage-dependent calcium channel gamma-2 subunit × 4 (Q71RJ2) E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–882; UniProt 21–902 Author chain B; PDBConstruct 1–882; UniProt 21–902 Author chain C; PDBConstruct 1–882; UniProt 21–902 Author chain D; PDBConstruct 1–882; UniProt 21–902

Voltage-dependent calcium channel gamma-2 subunit

Rattus norvegicus

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–323 Chain F; UniProt 1–323 Chain G; UniProt 1–323 Chain H; UniProt 1–323 Not recorded Isoform 2 of Glutamate receptor 4 × 4 (P19493) E2Q 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 2
Chains and sequence ranges Author chain E; PDBConstruct 1–323; UniProt 1–323 Author chain F; PDBConstruct 1–323; UniProt 1–323 Author chain G; PDBConstruct 1–323; UniProt 1–323 Author chain H; PDBConstruct 1–323; UniProt 1–323

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 9rms

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9rms
Deposition date deposition_date2025-06-18
Structure title titleGluA4 in complex with TARP-2, Resting II state, structure of TMD/LBD domains
Keywords keywordsGria4, Voltage-dependent calcium channel gamma-2, AMPA Receptor, GluA4-TARP2, Membrane protein, Resting state II, TMD/LBD; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.63
Radius of gyration Rg (electron density) rg_electron45.06
Forward intensity I(0) i0855714000.00
Molecular weight molecular_weight256490.0 kDa
Excluded volume excluded_volume326820 ų
Envelope volume envelope_volume468440 ų
Hydration-shell volume shell_volume84876 ų
Envelope diameter envelope_diameter149.1
Shell Rg shell_rg51.34
Envelope Rg envelope_rg43.88
Shape Rg shape_rg45.05
Total Rg total_rg45.40
Total atoms total_atoms18061
Residues n_residues2324
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 dmax145.9
Rg (real space) rg_real45.38
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real8.5570e+08
I(0) uncertainty (real space) i0_real_error1.4320e+07
Rg (reciprocal space) rg_reciprocal45.63
I(0) (reciprocal space) i0_reciprocal856000000.0000
Solution quality estimate total_estimate0.8897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.3
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63700000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)