8fp4

GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 500mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na610)

Method: ELECTRON MICROSCOPY Dmax: 115.1 Å Quality: GOOD

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

Glutamate receptor 2

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 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–883 Chain B; UniProt 1–883 Chain C; UniProt 1–883 Chain D; UniProt 1–883 Fragment:DYKDDDDK near the C-terminal is a FLAG epitope tag used for purification Voltage-dependent calcium channel gamma-2 subunit × 4 (O88602) CL CHLORIDE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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 1–889; UniProt 1–883 Author chain B; PDBConstruct 1–889; UniProt 1–883 Author chain C; PDBConstruct 1–889; UniProt 1–883 Author chain D; PDBConstruct 1–889; UniProt 1–883

Voltage-dependent calcium channel gamma-2 subunit

Mus musculus

UniProt O88602

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 Mutation:K52E, K53E Glutamate receptor 2 × 4 (P19491) CL CHLORIDE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;L-glutamic acid (100mM) and cyclothiazide (CTZ, 0.33mM) was added before freezing. The 1M L-glutamic acid stock solution is adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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.

39 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG2_MOUSE
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 8fp4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fp4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fp4
Deposition date deposition_date2023-01-04
Structure title titleGluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 500mM NaCl, 330uM CTZ, and 100mM glutamate (Open-Na610)
Keywords keywordsionotropic glutamate receptor, ligand gated ion channel, AMPA receptor, TARP gamma-2, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.82
Radius of gyration Rg (electron density) rg_electron35.46
Forward intensity I(0) i0300647000.00
Molecular weight molecular_weight150450.0 kDa
Excluded volume excluded_volume192140 ų
Envelope volume envelope_volume251230 ų
Hydration-shell volume shell_volume56798 ų
Envelope diameter envelope_diameter115.6
Shell Rg shell_rg43.52
Envelope Rg envelope_rg35.71
Shape Rg shape_rg35.41
Total Rg total_rg36.23
Total atoms total_atoms10616
Residues n_residues1365
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 dmax115.1
Rg (real space) rg_real36.56
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real3.0060e+08
I(0) uncertainty (real space) i0_real_error4.3950e+06
Rg (reciprocal space) rg_reciprocal36.73
I(0) (reciprocal space) i0_reciprocal300700000.0000
Solution quality estimate total_estimate0.8903
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.073
Kurtosis Kurtosis kurtosis-0.435
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25690000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)