8fph

Conformation 2 of the ligand binding domain (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg)

Method: ELECTRON MICROSCOPY Dmax: 112.8 Å Quality: EXCELLENT

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) 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 Mutation:FLAG epitope tag (DYKDDDDK) insertion GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;L-glutamic acid (100 mM) and cyclothiazide (CTZ, 330 uM) were added before freezing. The 1 M L-glutamic acid stock solution was adjusted to pH 7.4 using NaOH. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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

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 8fph

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8fph
Deposition date deposition_date2023-01-04
Structure title titleConformation 2 of the ligand binding domain (LBDconf2) of GluA2 flip Q isoform of AMPA receptor in complex with gain-of-function TARP gamma-2, with 10mM CaCl2, 150mM NaCl, 1mM MgCl2, 330uM CTZ, and 100mM glutamate (Open-CaNaMg)
Keywords keywords;ionotropic glutamate receptors, AMPA receptors, ion channel, ligand-gated ion channel, auxiliary subunit, stargazing, TARP gamma2, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.50
Radius of gyration Rg (electron density) rg_electron34.91
Forward intensity I(0) i0214677000.00
Molecular weight molecular_weight119730.0 kDa
Excluded volume excluded_volume150790 ų
Envelope volume envelope_volume202670 ų
Hydration-shell volume shell_volume47453 ų
Envelope diameter envelope_diameter121.3
Shell Rg shell_rg42.33
Envelope Rg envelope_rg34.18
Shape Rg shape_rg34.92
Total Rg total_rg35.43
Total atoms total_atoms8382
Residues n_residues1060
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 dmax112.8
Rg (real space) rg_real35.43
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real2.1470e+08
I(0) uncertainty (real space) i0_real_error3.1370e+06
Rg (reciprocal space) rg_reciprocal35.47
I(0) (reciprocal space) i0_reciprocal214700000.0000
Solution quality estimate total_estimate0.9066
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary110.3
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.573
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46730000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.941

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)