8ss3

Structure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to competitive antagonist ZK and channel blocker spermidine (closed state)

Method: ELECTRON MICROSCOPY Dmax: 150.1 Å Quality: REASONABLE

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) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 50 CLR CHOLESTEROL × 4 AJP Digitonin × 6 SPD SPERMIDINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.21 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) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 50 CLR CHOLESTEROL × 4 AJP Digitonin × 6 SPD SPERMIDINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.21 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) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 50 CLR CHOLESTEROL × 4 AJP Digitonin × 6 SPD SPERMIDINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.21 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 8ss3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ss3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ss3
Deposition date deposition_date2023-05-08
Structure title titleStructure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunits TARP gamma-5 and cornichon-2 bound to competitive antagonist ZK and channel blocker spermidine (closed 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_guinier45.85
Radius of gyration Rg (electron density) rg_electron45.13
Forward intensity I(0) i0891788000.00
Molecular weight molecular_weight283050.0 kDa
Excluded volume excluded_volume368930 ų
Envelope volume envelope_volume493570 ų
Hydration-shell volume shell_volume88232 ų
Envelope diameter envelope_diameter153.9
Shell Rg shell_rg51.90
Envelope Rg envelope_rg44.63
Shape Rg shape_rg45.12
Total Rg total_rg45.45
Total atoms total_atoms19887
Residues n_residues2280
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 dmax150.1
Rg (real space) rg_real45.67
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real8.9180e+08
I(0) uncertainty (real space) i0_real_error1.5930e+07
Rg (reciprocal space) rg_reciprocal45.85
I(0) (reciprocal space) i0_reciprocal892000000.0000
Solution quality estimate total_estimate0.6609
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.4
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha103400000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 0.021; Positv: 1.000; Valcen: 0.978; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)