5ide

Cryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model I)

Method: ELECTRON MICROSCOPY Dmax: 171.7 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 23–883 Chain C; UniProt 23–883 Mutation:N292C Glutamate receptor 3 × 2 (P19492) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;25 mM Tris pH 7.4, 0.25 % DDM, 150 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE;Incubated for 1 minute, blotted for 3 seconds Resolution 8.25 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 12–872; UniProt 23–883 Author chain C; PDBConstruct 12–872; UniProt 23–883

Glutamate receptor 3

Rattus norvegicus

UniProt P19492

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 24–888 Chain D; UniProt 24–888 Mutation:R439G, R265C Glutamate receptor 2 × 2 (P19491) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;25 mM Tris pH 7.4, 0.25 % DDM, 150 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE;Incubated for 1 minute, blotted for 3 seconds Resolution 8.25 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.

32 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA3_RAT
Isoform P19492-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 10–874; UniProt 24–888 Author chain D; PDBConstruct 10–874; UniProt 24–888

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 5ide

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ide
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ide
Deposition date deposition_date2016-02-24
Structure title titleCryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model I)
Keywords keywordsAMPA glutamate receptor, Signaling protein; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.07
Radius of gyration Rg (electron density) rg_electron49.94
Forward intensity I(0) i01037570000.00
Molecular weight molecular_weight164710.0 kDa
Excluded volume excluded_volume162250 ų
Envelope volume envelope_volume466650 ų
Hydration-shell volume shell_volume80248 ų
Envelope diameter envelope_diameter171.7
Shell Rg shell_rg53.35
Envelope Rg envelope_rg47.14
Shape Rg shape_rg49.94
Total Rg total_rg50.07
Total atoms total_atoms11746
Residues n_residues2937
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 dmax171.7
Rg (real space) rg_real50.04
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.0380e+09
I(0) uncertainty (real space) i0_real_error1.9910e+07
Rg (reciprocal space) rg_reciprocal50.09
I(0) (reciprocal space) i0_reciprocal1038000000.0000
Solution quality estimate total_estimate0.8566
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.9
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.158
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha124900000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.791

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)