9e4z

GluA2-gamma2 complex bound glutamate and cyclothiazide

Method: ELECTRON MICROSCOPY Dmax: 207.3 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 25–841 Chain B; UniProt 25–841 Chain C; UniProt 25–841 Chain D; UniProt 25–841 Not recorded Voltage-dependent calcium channel gamma-2 subunit × 4 (O88602) GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 1–811; UniProt 25–841 Author chain B; PDBConstruct 1–811; UniProt 25–841 Author chain C; PDBConstruct 1–811; UniProt 25–841 Author chain D; PDBConstruct 1–811; UniProt 25–841

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 3–208 Chain F; UniProt 3–208 Chain G; UniProt 3–208 Chain H; UniProt 3–208 Not recorded Isoform Flip of Glutamate receptor 2 × 4 (P19491) GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 1–206; UniProt 3–208 Author chain F; PDBConstruct 1–206; UniProt 3–208 Author chain G; PDBConstruct 1–206; UniProt 3–208 Author chain H; PDBConstruct 1–206; UniProt 3–208

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 9e4z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e4z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e4z
Deposition date deposition_date2024-10-25
Structure title titleGluA2-gamma2 complex bound glutamate and cyclothiazide
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_guinier61.17
Radius of gyration Rg (electron density) rg_electron61.35
Forward intensity I(0) i02601530000.00
Molecular weight molecular_weight442610.0 kDa
Excluded volume excluded_volume559320 ų
Envelope volume envelope_volume826280 ų
Hydration-shell volume shell_volume116080 ų
Envelope diameter envelope_diameter200.9
Shell Rg shell_rg59.59
Envelope Rg envelope_rg59.57
Shape Rg shape_rg61.39
Total Rg total_rg61.15
Total atoms total_atoms31168
Residues n_residues3950
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 dmax207.3
Rg (real space) rg_real61.30
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real2.6020e+09
I(0) uncertainty (real space) i0_real_error5.3520e+07
Rg (reciprocal space) rg_reciprocal61.03
I(0) (reciprocal space) i0_reciprocal2600000000.0000
Solution quality estimate total_estimate0.8135
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.8
Skewness Skewness skewness0.374
Kurtosis Kurtosis kurtosis-0.425
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha184800000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)