8piv

Homomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, desensitized conformation 1

Method: ELECTRON MICROSCOPY Dmax: 139.2 Å Quality: GOOD

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

Glutamate receptor

Rattus norvegicus

UniProt G3V914

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 1–883 Chain B; UniProt 1–883 Chain C; UniProt 1–883 Chain D; UniProt 1–883 Not recorded Voltage-dependent calcium channel gamma-2 subunit × 4 (Q71RJ2) PLM PALMITIC ACID × 7 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name G3V914_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–883; UniProt 1–883 Author chain B; PDBConstruct 1–883; UniProt 1–883 Author chain C; PDBConstruct 1–883; UniProt 1–883 Author chain D; PDBConstruct 1–883; UniProt 1–883

Voltage-dependent calcium channel gamma-2 subunit

Rattus norvegicus

UniProt Q71RJ2

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 1–323 Chain F; UniProt 1–323 Chain G; UniProt 1–323 Chain H; UniProt 1–323 Not recorded Glutamate receptor × 4 (G3V914) PLM PALMITIC ACID × 7 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–323; UniProt 1–323 Author chain F; PDBConstruct 1–323; UniProt 1–323 Author chain G; PDBConstruct 1–323; UniProt 1–323 Author chain H; PDBConstruct 1–323; UniProt 1–323

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 8piv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8piv
Deposition date deposition_date2023-06-22
Structure title titleHomomeric GluA2 flip R/G-unedited Q/R-edited F231A mutant in tandem with TARP gamma-2, 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_guinier46.05
Radius of gyration Rg (electron density) rg_electron45.10
Forward intensity I(0) i0818988000.00
Molecular weight molecular_weight255900.0 kDa
Excluded volume excluded_volume328010 ų
Envelope volume envelope_volume462960 ų
Hydration-shell volume shell_volume83938 ų
Envelope diameter envelope_diameter146.4
Shell Rg shell_rg51.48
Envelope Rg envelope_rg43.63
Shape Rg shape_rg45.09
Total Rg total_rg45.41
Total atoms total_atoms18017
Residues n_residues2293
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 dmax139.2
Rg (real space) rg_real45.75
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real8.1900e+08
I(0) uncertainty (real space) i0_real_error1.4910e+07
Rg (reciprocal space) rg_reciprocal46.05
I(0) (reciprocal space) i0_reciprocal819300000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.3
Skewness Skewness skewness0.094
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45860000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.560

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8pivE01
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_id8pivF01
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_id8pivG01
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_id8pivH01
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)