7ryy

Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist glutamate

Method: ELECTRON MICROSCOPY Dmax: 130.9 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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) 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 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 GLU GLUTAMIC ACID × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;25 mM glutamate was added to the purified protein and incubated on ice for 30 min before sample preparation Resolution 4.40 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
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

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 7ryy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ryy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ryy
Deposition date deposition_date2021-08-26
Structure title titleStructure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist glutamate
Keywords keywordsAMPA receptor, ion channel, neurotransmission, synapse, TARP gamma-5, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.63
Radius of gyration Rg (electron density) rg_electron43.31
Forward intensity I(0) i0666294000.00
Molecular weight molecular_weight225230.0 kDa
Excluded volume excluded_volume287150 ų
Envelope volume envelope_volume405590 ų
Hydration-shell volume shell_volume76891 ų
Envelope diameter envelope_diameter135.5
Shell Rg shell_rg49.20
Envelope Rg envelope_rg42.50
Shape Rg shape_rg43.31
Total Rg total_rg43.61
Total atoms total_atoms15836
Residues n_residues2020
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 dmax130.9
Rg (real space) rg_real43.43
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real6.6630e+08
I(0) uncertainty (real space) i0_real_error1.1670e+07
Rg (reciprocal space) rg_reciprocal43.63
I(0) (reciprocal space) i0_reciprocal666400000.0000
Solution quality estimate total_estimate0.8743
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.5
Skewness Skewness skewness0.127
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha109900000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.976; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.451

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)