9rn7

GluA4 in complex with TARP-2, Desensitized state, structure of TMD domain

Method: ELECTRON MICROSCOPY Dmax: 109.6 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) PLM PALMITIC ACID × 4 CA CALCIUM ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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) PLM PALMITIC ACID × 4 CA CALCIUM ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 9rn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rn7
Deposition date deposition_date2025-06-19
Structure title titleGluA4 in complex with TARP-2, Desensitized state, structure of TMD domain
Keywords keywordsGria4, Voltage-dependent calcium channel gamma-2, AMPA Receptor, GluA4-TARP2, Membrane protein, Desensitized state, TMD; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.25
Radius of gyration Rg (electron density) rg_electron34.86
Forward intensity I(0) i0268822000.00
Molecular weight molecular_weight146450.0 kDa
Excluded volume excluded_volume188860 ų
Envelope volume envelope_volume241440 ų
Hydration-shell volume shell_volume55852 ų
Envelope diameter envelope_diameter116.5
Shell Rg shell_rg42.69
Envelope Rg envelope_rg35.19
Shape Rg shape_rg34.82
Total Rg total_rg35.59
Total atoms total_atoms10340
Residues n_residues1315
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 dmax109.6
Rg (real space) rg_real36.03
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real2.6880e+08
I(0) uncertainty (real space) i0_real_error4.3780e+06
Rg (reciprocal space) rg_reciprocal36.17
I(0) (reciprocal space) i0_reciprocal268900000.0000
Solution quality estimate total_estimate0.8905
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.3
Skewness Skewness skewness0.106
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha21380000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)