9qfh

The composite map of of the AMPAR complex GluA3- TARP gamma2 in the apo state.

Method: ELECTRON MICROSCOPY Dmax: 226.2 Å Quality: GOOD

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

Isoform Flip of Glutamate receptor 3,Voltage-dependent calcium channel gamma-2 subunit

Rattus norvegicus

UniProt P19492

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 24–865 Chain B; UniProt 24–865 Chain C; UniProt 24–865 Chain D; UniProt 24–865 Chain W; UniProt 24–865 Chain X; UniProt 24–865 Chain Y; UniProt 24–865 Chain Z; UniProt 24–865 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA3_RAT
Isoform P19492-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–842; UniProt 24–865 Author chain B; PDBConstruct 1–842; UniProt 24–865 Author chain C; PDBConstruct 1–842; UniProt 24–865 Author chain D; PDBConstruct 1–842; UniProt 24–865 Author chain W; PDBConstruct 1–842; UniProt 24–865 Author chain X; PDBConstruct 1–842; UniProt 24–865 Author chain Y; PDBConstruct 1–842; UniProt 24–865 Author chain Z; PDBConstruct 1–842; UniProt 24–865

Isoform Flip of Glutamate receptor 3,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 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 2–323 Chain B; UniProt 2–323 Chain C; UniProt 2–323 Chain D; UniProt 2–323 Chain W; UniProt 2–323 Chain X; UniProt 2–323 Chain Y; UniProt 2–323 Chain Z; UniProt 2–323 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 A; PDBConstruct 849–1170; UniProt 2–323 Author chain B; PDBConstruct 849–1170; UniProt 2–323 Author chain C; PDBConstruct 849–1170; UniProt 2–323 Author chain D; PDBConstruct 849–1170; UniProt 2–323 Author chain W; PDBConstruct 849–1170; UniProt 2–323 Author chain X; PDBConstruct 849–1170; UniProt 2–323 Author chain Y; PDBConstruct 849–1170; UniProt 2–323 Author chain Z; PDBConstruct 849–1170; UniProt 2–323

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 9qfh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qfh
Deposition date deposition_date2025-03-11
Structure title titleThe composite map of of the AMPAR complex GluA3- TARP gamma2 in the apo state.
Keywords keywordsAMPAR, ion channels, neurotransmission, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.37
Radius of gyration Rg (electron density) rg_electron64.46
Forward intensity I(0) i02300120000.00
Molecular weight molecular_weight419360.0 kDa
Excluded volume excluded_volume530870 ų
Envelope volume envelope_volume791470 ų
Hydration-shell volume shell_volume108810 ų
Envelope diameter envelope_diameter210.8
Shell Rg shell_rg58.86
Envelope Rg envelope_rg62.45
Shape Rg shape_rg64.51
Total Rg total_rg64.16
Total atoms total_atoms29581
Residues n_residues3759
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 dmax226.2
Rg (real space) rg_real64.49
Rg uncertainty (real space) rg_real_error2.72
I(0) (real space) i0_real2.3000e+09
I(0) uncertainty (real space) i0_real_error5.1830e+07
Rg (reciprocal space) rg_reciprocal64.22
I(0) (reciprocal space) i0_reciprocal2299000000.0000
Solution quality estimate total_estimate0.8139
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.4
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.598
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha136200000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)