6ud8

GluA2 in complex with its auxiliary subunit CNIH3 - with antagonist ZK200775

Method: ELECTRON MICROSCOPY Dmax: 155.0 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 1–868 Chain B; UniProt 1–868 Chain C; UniProt 1–868 Chain D; UniProt 1–868 Not recorded Protein cornichon homolog 3 × 4 (Q6ZWS4) OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 CLR CHOLESTEROL × 4 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–868; UniProt 1–868 Author chain B; PDBConstruct 1–868; UniProt 1–868 Author chain C; PDBConstruct 1–868; UniProt 1–868 Author chain D; PDBConstruct 1–868; UniProt 1–868

Protein cornichon homolog 3

Mus musculus

UniProt Q6ZWS4

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 1–160 Chain F; UniProt 1–160 Chain G; UniProt 1–160 Chain H; UniProt 1–160 Not recorded Glutamate receptor 2 × 4 (P19491) OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 CLR CHOLESTEROL × 4 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNIH3_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–160; UniProt 1–160 Author chain F; PDBConstruct 1–160; UniProt 1–160 Author chain G; PDBConstruct 1–160; UniProt 1–160 Author chain H; PDBConstruct 1–160; UniProt 1–160

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 6ud8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ud8
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6ud8
Deposition date deposition_date2019-09-18
Structure title titleGluA2 in complex with its auxiliary subunit CNIH3 - with antagonist ZK200775
Keywords keywords;ionotropic glutamate receptor, AMPA receptor, cornichon, auxiliary subunit, ion channel, ligand gated ion channel, synaptic transmission, excitatory synaptic transmission, neurotransmitter receptor, stargazin, TARP, lipid, MPQX, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.35
Radius of gyration Rg (electron density) rg_electron46.62
Forward intensity I(0) i0653476000.00
Molecular weight molecular_weight229840.0 kDa
Excluded volume excluded_volume294670 ų
Envelope volume envelope_volume410040 ų
Hydration-shell volume shell_volume73047 ų
Envelope diameter envelope_diameter148.0
Shell Rg shell_rg50.71
Envelope Rg envelope_rg45.91
Shape Rg shape_rg46.62
Total Rg total_rg46.77
Total atoms total_atoms32056
Residues n_residues2042
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 dmax155.0
Rg (real space) rg_real47.27
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real6.5350e+08
I(0) uncertainty (real space) i0_real_error1.0490e+07
Rg (reciprocal space) rg_reciprocal47.35
I(0) (reciprocal space) i0_reciprocal653500000.0000
Solution quality estimate total_estimate0.8968
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.4
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62250000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)