4uqj

Cryo-EM density map of GluA2em in complex with ZK200775

Method: ELECTRON MICROSCOPY Dmax: 200.9 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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 22–847 Chain B; UniProt 22–847 Chain C; UniProt 22–847 Chain D; UniProt 22–847 Fragment:RESIDUES 22-847 Mutation:YES ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY cryo-EM buffer:150 MM NACL, 20 MM TRIS, 0.75 MM DDM, 0.12 MM CHS, 0.3 MM ZK200775;pH 8;150 MM NACL, 20 MM TRIS, 0.75 MM DDM, 0.12 MM CHS, 0.3 MM ZK200775 cryo-EM vitrification conditions:Cryogen ETHANE;ETHANE Resolution 10.40 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 1–826; UniProt 22–847 Author chain B; PDBConstruct 1–826; UniProt 22–847 Author chain C; PDBConstruct 1–826; UniProt 22–847 Author chain D; PDBConstruct 1–826; UniProt 22–847

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 4uqj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4uqj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4uqj
Deposition date deposition_date2014-06-24
Structure title titleCryo-EM density map of GluA2em in complex with ZK200775
Keywords keywordsTRANSPORT PROTEIN, GLUA2EM ANTAGONIST-BOUND CLOSED STATE; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.34
Radius of gyration Rg (electron density) rg_electron59.75
Forward intensity I(0) i01296710000.00
Molecular weight molecular_weight308520.0 kDa
Excluded volume excluded_volume387340 ų
Envelope volume envelope_volume607300 ų
Hydration-shell volume shell_volume86641 ų
Envelope diameter envelope_diameter199.1
Shell Rg shell_rg60.41
Envelope Rg envelope_rg57.85
Shape Rg shape_rg59.78
Total Rg total_rg59.65
Total atoms total_atoms21793
Residues n_residues2983
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 dmax200.9
Rg (real space) rg_real59.42
Rg uncertainty (real space) rg_real_error2.17
I(0) (real space) i0_real1.2970e+09
I(0) uncertainty (real space) i0_real_error2.7300e+07
Rg (reciprocal space) rg_reciprocal59.26
I(0) (reciprocal space) i0_reciprocal1296000000.0000
Solution quality estimate total_estimate0.8453
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.3
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55550000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.437

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)