8p3t

Homomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 1

Method: ELECTRON MICROSCOPY Dmax: 143.6 Å Quality: REASONABLE

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

Glutamate receptor 1 flip isoform

Rattus norvegicus

UniProt P19490

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 1–907 Chain B; UniProt 1–907 Chain C; UniProt 1–907 Chain D; UniProt 1–907 Not recorded Voltage-dependent calcium channel gamma-3 subunit × 4 (Q8VHX0) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA1_RAT
Isoform P19490-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–915; UniProt 1–907 Author chain B; PDBConstruct 1–915; UniProt 1–907 Author chain C; PDBConstruct 1–915; UniProt 1–907 Author chain D; PDBConstruct 1–915; UniProt 1–907

Voltage-dependent calcium channel gamma-3 subunit

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 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 2–315 Chain F; UniProt 2–315 Chain G; UniProt 2–315 Chain H; UniProt 2–315 Not recorded Glutamate receptor 1 flip isoform × 4 (P19490) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 2
Chains and sequence ranges Author chain E; PDBConstruct 1–314; UniProt 2–315 Author chain F; PDBConstruct 1–314; UniProt 2–315 Author chain G; PDBConstruct 1–314; UniProt 2–315 Author chain H; PDBConstruct 1–314; UniProt 2–315

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 8p3t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p3t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p3t
Deposition date deposition_date2023-05-18
Structure title titleHomomeric GluA1 in tandem with TARP gamma-3, desensitized conformation 1
Keywords keywordsAMPAR, ion channels, neurotransmission, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.96
Radius of gyration Rg (electron density) rg_electron45.18
Forward intensity I(0) i0728770000.00
Molecular weight molecular_weight237870.0 kDa
Excluded volume excluded_volume303410 ų
Envelope volume envelope_volume435800 ų
Hydration-shell volume shell_volume78967 ų
Envelope diameter envelope_diameter142.6
Shell Rg shell_rg51.30
Envelope Rg envelope_rg43.77
Shape Rg shape_rg45.18
Total Rg total_rg45.46
Total atoms total_atoms16799
Residues n_residues2237
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 dmax143.6
Rg (real space) rg_real45.68
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real7.2880e+08
I(0) uncertainty (real space) i0_real_error1.4060e+07
Rg (reciprocal space) rg_reciprocal45.96
I(0) (reciprocal space) i0_reciprocal729000000.0000
Solution quality estimate total_estimate0.6813
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.1
Skewness Skewness skewness0.103
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40720000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.963; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8p3tE01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150
Domain ID domain_id8p3tF01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150
Domain ID domain_id8p3tG01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150
Domain ID domain_id8p3tH01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150

8. Citations (1)

9. Files and Curves (10)