7tnk

Complex GNNN of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM)

Method: ELECTRON MICROSCOPY Dmax: 143.0 Å Quality: GOOD

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

Isoform Flip of Glutamate receptor 2,Voltage-dependent calcium channel gamma-3 subunit chimera

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 Insufficient information 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 GLU GLUTAMIC ACID × 1 CYZ CYCLOTHIAZIDE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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 1–817; 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

Isoform Flip of Glutamate receptor 2,Voltage-dependent calcium channel gamma-3 subunit chimera

Rattus norvegicus

UniProt Q8VHX0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 5–207 Chain B; UniProt 5–207 Chain C; UniProt 5–207 Chain D; UniProt 5–207 Not recorded GLU GLUTAMIC ACID × 1 CYZ CYCLOTHIAZIDE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG3_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 823–1026; UniProt 5–207 Author chain B; PDBConstruct 823–1026; UniProt 5–207 Author chain C; PDBConstruct 823–1026; UniProt 5–207 Author chain D; PDBConstruct 823–1026; UniProt 5–207

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 7tnk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7tnk
Deposition date deposition_date2022-01-21
Structure title titleComplex GNNN of AMPA-subtype iGluR GluA2 in complex with auxiliary subunit gamma2 (Stargazin) at low glutamate concentration (20 uM) in the presence of cyclothiazide (100 uM)
Keywords keywords;AMPA, iGluR, Stargazin, cryo-EM, complex, agonist, positive allosteric modulator, subconductance level, opening, gating, glutamate, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.00
Radius of gyration Rg (electron density) rg_electron44.45
Forward intensity I(0) i0961021000.00
Molecular weight molecular_weight269320.0 kDa
Excluded volume excluded_volume342290 ų
Envelope volume envelope_volume486260 ų
Hydration-shell volume shell_volume88309 ų
Envelope diameter envelope_diameter144.9
Shell Rg shell_rg51.49
Envelope Rg envelope_rg43.50
Shape Rg shape_rg44.44
Total Rg total_rg44.83
Total atoms total_atoms18934
Residues n_residues2418
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 dmax143.0
Rg (real space) rg_real44.76
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real9.6100e+08
I(0) uncertainty (real space) i0_real_error1.7160e+07
Rg (reciprocal space) rg_reciprocal45.00
I(0) (reciprocal space) i0_reciprocal961300000.0000
Solution quality estimate total_estimate0.8900
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.2
Skewness Skewness skewness0.155
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha100000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.874

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)