9dhr

Glutamate activated state of the GluA2-gamma2 complex

Method: ELECTRON MICROSCOPY Dmax: 149.1 Å Quality: GOOD

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

Isoform Flip of 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 412–841 Chain B; UniProt 412–841 Chain C; UniProt 412–841 Chain D; UniProt 412–841 Not recorded Voltage-dependent calcium channel gamma-2 subunit × 4 (O88602) GLU GLUTAMIC ACID × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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 1–430; UniProt 412–841 Author chain B; PDBConstruct 1–430; UniProt 412–841 Author chain C; PDBConstruct 1–430; UniProt 412–841 Author chain D; PDBConstruct 1–430; UniProt 412–841

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 6–208 Chain F; UniProt 6–208 Chain G; UniProt 6–208 Chain H; UniProt 6–208 Not recorded Isoform Flip of Glutamate receptor 2 × 4 (P19491) GLU GLUTAMIC ACID × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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 1–203; UniProt 6–208 Author chain F; PDBConstruct 1–203; UniProt 6–208 Author chain G; PDBConstruct 1–203; UniProt 6–208 Author chain H; PDBConstruct 1–203; UniProt 6–208

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 9dhr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dhr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9dhr
Deposition date deposition_date2024-09-04
Structure title titleGlutamate activated state of the GluA2-gamma2 complex
Keywords keywordsligand-gated ion channel, ionotropic glutamate receptor, ampa receptor, ion channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.25
Radius of gyration Rg (electron density) rg_electron46.61
Forward intensity I(0) i0887074000.00
Molecular weight molecular_weight260140.0 kDa
Excluded volume excluded_volume331170 ų
Envelope volume envelope_volume501890 ų
Hydration-shell volume shell_volume88299 ų
Envelope diameter envelope_diameter155.7
Shell Rg shell_rg52.66
Envelope Rg envelope_rg45.07
Shape Rg shape_rg46.59
Total Rg total_rg46.95
Total atoms total_atoms18298
Residues n_residues2346
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 dmax149.1
Rg (real space) rg_real46.96
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real8.8710e+08
I(0) uncertainty (real space) i0_real_error1.5520e+07
Rg (reciprocal space) rg_reciprocal47.25
I(0) (reciprocal space) i0_reciprocal887400000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.7
Skewness Skewness skewness0.114
Kurtosis Kurtosis kurtosis-0.523
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76010000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)