8ss5

Structure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunit TARP gamma-5 (apo state)

Method: ELECTRON MICROSCOPY Dmax: 143.0 Å Quality: GOOD

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

Glutamate receptor 2, Voltage-dependent calcium channel gamma-5 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 NA SODIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.56 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

Glutamate receptor 2, Voltage-dependent calcium channel gamma-5 subunit chimera

Rattus norvegicus

UniProt Q8VHW8

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 4–207 Chain B; UniProt 4–207 Chain C; UniProt 4–207 Chain D; UniProt 4–207 Not recorded NA SODIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 3.56 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 823–1026; UniProt 4–207 Author chain B; PDBConstruct 823–1026; UniProt 4–207 Author chain C; PDBConstruct 823–1026; UniProt 4–207 Author chain D; PDBConstruct 823–1026; UniProt 4–207

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 8ss5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ss5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ss5
Deposition date deposition_date2023-05-08
Structure title titleStructure of LBD-TMD of AMPA receptor GluA2 in complex with auxiliary subunit TARP gamma-5 (apo state)
Keywords keywordsAMPA receptor, neurotransmission, TARP gamma-5, Ion-channel, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.01
Radius of gyration Rg (electron density) rg_electron43.61
Forward intensity I(0) i0643021000.00
Molecular weight molecular_weight222250.0 kDa
Excluded volume excluded_volume283710 ų
Envelope volume envelope_volume399370 ų
Hydration-shell volume shell_volume75544 ų
Envelope diameter envelope_diameter140.1
Shell Rg shell_rg49.16
Envelope Rg envelope_rg42.81
Shape Rg shape_rg43.61
Total Rg total_rg43.90
Total atoms total_atoms15637
Residues n_residues1998
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_real43.84
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real6.4300e+08
I(0) uncertainty (real space) i0_real_error1.1800e+07
Rg (reciprocal space) rg_reciprocal44.00
I(0) (reciprocal space) i0_reciprocal643100000.0000
Solution quality estimate total_estimate0.8260
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.6
Skewness Skewness skewness0.155
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha126900000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)