5idf

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

Method: ELECTRON MICROSCOPY Dmax: 181.3 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 Not recorded 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 10.31 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 Not recorded 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 10.31 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 5idf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5idf
Deposition date deposition_date2016-02-24
Structure title titleCryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model II)
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_guinier52.16
Radius of gyration Rg (electron density) rg_electron52.13
Forward intensity I(0) i01042930000.00
Molecular weight molecular_weight165270.0 kDa
Excluded volume excluded_volume162780 ų
Envelope volume envelope_volume481280 ų
Hydration-shell volume shell_volume80904 ų
Envelope diameter envelope_diameter182.4
Shell Rg shell_rg54.33
Envelope Rg envelope_rg48.32
Shape Rg shape_rg52.13
Total Rg total_rg52.21
Total atoms total_atoms11786
Residues n_residues2947
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 dmax181.3
Rg (real space) rg_real52.18
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real1.0430e+09
I(0) uncertainty (real space) i0_real_error2.0310e+07
Rg (reciprocal space) rg_reciprocal52.14
I(0) (reciprocal space) i0_reciprocal1043000000.0000
Solution quality estimate total_estimate0.8429
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.5
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.091
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha85340000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.724; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.793

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)