8c1p

Active state homomeric GluA1 AMPA receptor in complex with TARP gamma 3

Method: ELECTRON MICROSCOPY Dmax: 142.8 Å Quality: GOOD

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) CYZ CYCLOTHIAZIDE × 4 PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 GLU GLUTAMIC ACID × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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) CYZ CYCLOTHIAZIDE × 4 PLM PALMITIC ACID × 6 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 GLU GLUTAMIC ACID × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 8c1p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8c1p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8c1p
Deposition date deposition_date2022-12-21
Structure title titleActive state homomeric GluA1 AMPA receptor in complex with TARP gamma 3
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_guinier45.35
Radius of gyration Rg (electron density) rg_electron44.54
Forward intensity I(0) i0799010000.00
Molecular weight molecular_weight250290.0 kDa
Excluded volume excluded_volume319750 ų
Envelope volume envelope_volume451180 ų
Hydration-shell volume shell_volume82725 ų
Envelope diameter envelope_diameter142.0
Shell Rg shell_rg51.43
Envelope Rg envelope_rg42.96
Shape Rg shape_rg44.56
Total Rg total_rg44.80
Total atoms total_atoms17644
Residues n_residues2296
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 dmax142.8
Rg (real space) rg_real45.05
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real7.9900e+08
I(0) uncertainty (real space) i0_real_error1.5390e+07
Rg (reciprocal space) rg_reciprocal45.35
I(0) (reciprocal space) i0_reciprocal799300000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.1
Skewness Skewness skewness0.066
Kurtosis Kurtosis kurtosis-0.521
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49920000.0000
Real-space data points n_real_points36
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: 0.979; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8c1pE01
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_id8c1pF01
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_id8c1pG01
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_id8c1pH01
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)