8ssa

Structure of AMPA receptor GluA2 complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to glutamate and channel blocker spermidine (desensitized state)

Method: ELECTRON MICROSCOPY Dmax: 208.2 Å Quality: GOOD

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

Glutamate receptor 2, Voltage-dependent calcium channel gamma-5 subunit chimera

Rattus norvegicus

UniProt P19491

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 Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 25–847 Chain B; UniProt 25–847 Chain C; UniProt 25–847 Chain D; UniProt 25–847 Not recorded Protein cornichon homolog 2 × 2 (Q6PI25) PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 12 GLU GLUTAMIC ACID × 4 SPD SPERMIDINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.88 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.

333 other PDB entries and 482 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA2_RAT
Isoform P19491-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–817; UniProt 25–847 Author chain B; PDBConstruct 1–817; UniProt 25–847 Author chain C; PDBConstruct 1–817; UniProt 25–847 Author chain D; PDBConstruct 1–817; UniProt 25–847

Glutamate receptor 2, Voltage-dependent calcium channel gamma-5 subunit chimera

Rattus norvegicus

UniProt Q8VHW8

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 Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 4–207 Chain B; UniProt 4–207 Chain C; UniProt 4–207 Chain D; UniProt 4–207 Not recorded Protein cornichon homolog 2 × 2 (Q6PI25) PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 12 GLU GLUTAMIC ACID × 4 SPD SPERMIDINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.88 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 CCG5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 823–1026; UniProt 4–207 Author chain B; PDBConstruct 823–1026; UniProt 4–207 Author chain C; PDBConstruct 823–1026; UniProt 4–207 Author chain D; PDBConstruct 823–1026; UniProt 4–207

Protein cornichon homolog 2

Homo sapiens

UniProt Q6PI25

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 Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–160 Chain F; UniProt 1–160 Not recorded Glutamate receptor 2, Voltage-dependent calcium channel gamma-5 subunit chimera × 4 (P19491,Q8VHW8) PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 12 GLU GLUTAMIC ACID × 4 SPD SPERMIDINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.88 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNIH2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–160; UniProt 1–160 Author chain F; PDBConstruct 1–160; UniProt 1–160

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 8ssa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ssa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ssa
Deposition date deposition_date2023-05-08
Structure title titleStructure of AMPA receptor GluA2 complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to glutamate and channel blocker spermidine (desensitized state)
Keywords keywordsAMPA receptor, spermidine, TARP gamma-5, cornichon-2, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.26
Radius of gyration Rg (electron density) rg_electron61.47
Forward intensity I(0) i02465110000.00
Molecular weight molecular_weight438710.0 kDa
Excluded volume excluded_volume557630 ų
Envelope volume envelope_volume808890 ų
Hydration-shell volume shell_volume113860 ų
Envelope diameter envelope_diameter205.8
Shell Rg shell_rg59.09
Envelope Rg envelope_rg59.86
Shape Rg shape_rg61.51
Total Rg total_rg61.28
Total atoms total_atoms30888
Residues n_residues3836
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 dmax208.2
Rg (real space) rg_real61.42
Rg uncertainty (real space) rg_real_error2.12
I(0) (real space) i0_real2.4650e+09
I(0) uncertainty (real space) i0_real_error5.3700e+07
Rg (reciprocal space) rg_reciprocal61.09
I(0) (reciprocal space) i0_reciprocal2464000000.0000
Solution quality estimate total_estimate0.8515
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.1
Skewness Skewness skewness0.391
Kurtosis Kurtosis kurtosis-0.391
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha169100000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.493

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)