8c1r

Resting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma-2

Method: ELECTRON MICROSCOPY Dmax: 144.4 Å Quality: GOOD

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

Glutamate receptor 2

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 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) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 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 3.20 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 1–891; UniProt 1–883 Author chain B; PDBConstruct 1–891; UniProt 1–883 Author chain C; PDBConstruct 1–891; UniProt 1–883 Author chain D; PDBConstruct 1–891; 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 2–323 Chain F; UniProt 2–323 Chain G; UniProt 2–323 Chain H; UniProt 2–323 Not recorded Glutamate receptor 2 × 4 (P19491) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 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 3.20 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 1–322; UniProt 2–323 Author chain F; PDBConstruct 1–322; UniProt 2–323 Author chain G; PDBConstruct 1–322; UniProt 2–323 Author chain H; PDBConstruct 1–322; UniProt 2–323

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 8c1r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8c1r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8c1r
Deposition date deposition_date2022-12-21
Structure title titleResting state homomeric GluA2 F231A mutant AMPA receptor in complex with TARP gamma-2
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_guinier45.18
Radius of gyration Rg (electron density) rg_electron44.40
Forward intensity I(0) i0854889000.00
Molecular weight molecular_weight259580.0 kDa
Excluded volume excluded_volume331910 ų
Envelope volume envelope_volume456220 ų
Hydration-shell volume shell_volume83491 ų
Envelope diameter envelope_diameter142.7
Shell Rg shell_rg50.87
Envelope Rg envelope_rg43.49
Shape Rg shape_rg44.42
Total Rg total_rg44.67
Total atoms total_atoms18272
Residues n_residues2331
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 dmax144.4
Rg (real space) rg_real44.96
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real8.5490e+08
I(0) uncertainty (real space) i0_real_error1.4240e+07
Rg (reciprocal space) rg_reciprocal45.18
I(0) (reciprocal space) i0_reciprocal855100000.0000
Solution quality estimate total_estimate0.8242
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.8
Skewness Skewness skewness0.150
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77040000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8c1rE01
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_id8c1rF01
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_id8c1rG01
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_id8c1rH01
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)