6njm

Architecture and subunit arrangement of native AMPA receptors

Method: ELECTRON MICROSCOPY Dmax: 227.0 Å Quality: GOOD

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

Glutamate receptor 3

OrganismNot specified

UniProt P19492

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 16 其他Polymer 6 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–888 Chain C; UniProt 1–888 Not recorded Glutamate receptor 2 × 2 (P19491) ;A'-C' auxiliary proteins ; × 2 Voltage-dependent calcium channel gamma-2 subunit × 2 (Q71RJ2) 5B2 Fab Light Chain × 2 5B2 Fab Heavy Chain × 2 15F1 Fab light chain × 2 15F1 Fab heavy chain × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA3_RAT
Isoform P19492-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–888; UniProt 1–888 Author chain C; PDBConstruct 1–888; UniProt 1–888

Glutamate receptor 2

OrganismNot specified

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 Other combination Heteromer Protein × 16 其他Polymer 6 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain B; UniProt 1–883 Chain D; UniProt 1–883 Not recorded Glutamate receptor 3 × 2 (P19492) ;A'-C' auxiliary proteins ; × 2 Voltage-dependent calcium channel gamma-2 subunit × 2 (Q71RJ2) 5B2 Fab Light Chain × 2 5B2 Fab Heavy Chain × 2 15F1 Fab light chain × 2 15F1 Fab heavy chain × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–883; UniProt 1–883 Author chain D; PDBConstruct 1–883; UniProt 1–883

Voltage-dependent calcium channel gamma-2 subunit

OrganismNot specified

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 Other combination Heteromer Protein × 16 其他Polymer 6 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain F; UniProt 1–323 Chain H; UniProt 1–323 Not recorded Glutamate receptor 3 × 2 (P19492) Glutamate receptor 2 × 2 (P19491) ;A'-C' auxiliary proteins ; × 2 5B2 Fab Light Chain × 2 5B2 Fab Heavy Chain × 2 15F1 Fab light chain × 2 15F1 Fab heavy chain × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 4
Chains and sequence ranges Author chain F; 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 6njm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6njm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6njm
Deposition date deposition_date2019-01-03
Structure title titleArchitecture and subunit arrangement of native AMPA receptors
Keywords keywordsAMPA receptor, ligand gated ion channel, neurotransmitter, synapse, MEMBRANE PROTEIN, MEMBRANE PROTEIN-Immune System complex; MEMBRANE PROTEIN/Immune System
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier75.66
Radius of gyration Rg (electron density) rg_electron75.07
Forward intensity I(0) i03839240000.00
Molecular weight molecular_weight500590.0 kDa
Excluded volume excluded_volume614250 ų
Envelope volume envelope_volume1169800 ų
Hydration-shell volume shell_volume132760 ų
Envelope diameter envelope_diameter262.6
Shell Rg shell_rg70.24
Envelope Rg envelope_rg74.43
Shape Rg shape_rg75.26
Total Rg total_rg74.34
Total atoms total_atoms35458
Residues n_residues5420
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 dmax227.0
Rg (real space) rg_real75.37
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real3.8220e+09
I(0) uncertainty (real space) i0_real_error8.2430e+07
Rg (reciprocal space) rg_reciprocal74.15
I(0) (reciprocal space) i0_reciprocal3824000000.0000
Solution quality estimate total_estimate0.8476
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.7
Skewness Skewness skewness0.490
Kurtosis Kurtosis kurtosis-0.307
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0319
Highest regularization parameter α highest_alpha191100000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.189

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)