8fwt

Structure of the amino terminal domain of kainate receptor GluK2 in complex with the positive allosteric modulator BPAM344 and competitive antagonist DNQX

Method: ELECTRON MICROSCOPY Dmax: 157.5 Å Quality: GOOD

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

Glutamate receptor ionotropic, kainate 2

Rattus norvegicus

UniProt P42260

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 Homooligomer Protein × 4 其他Polymer 8 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–908 Chain B; UniProt 1–908 Chain C; UniProt 1–908 Chain D; UniProt 1–908 Not recorded beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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.

91 other PDB entries and 106 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIK2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–908; UniProt 1–908 Author chain B; PDBConstruct 1–908; UniProt 1–908 Author chain C; PDBConstruct 1–908; UniProt 1–908 Author chain D; PDBConstruct 1–908; UniProt 1–908

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 8fwt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8fwt
Deposition date deposition_date2023-01-23
Structure title titleStructure of the amino terminal domain of kainate receptor GluK2 in complex with the positive allosteric modulator BPAM344 and competitive antagonist DNQX
Keywords keywordsiGluR, Kainate receptor, positive allosteric modulator, DNQX, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.34
Radius of gyration Rg (electron density) rg_electron46.34
Forward intensity I(0) i0459199000.00
Molecular weight molecular_weight179240.0 kDa
Excluded volume excluded_volume225120 ų
Envelope volume envelope_volume307430 ų
Hydration-shell volume shell_volume56350 ų
Envelope diameter envelope_diameter157.3
Shell Rg shell_rg49.09
Envelope Rg envelope_rg45.74
Shape Rg shape_rg46.33
Total Rg total_rg46.48
Total atoms total_atoms12606
Residues n_residues1532
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 dmax157.5
Rg (real space) rg_real46.62
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real4.5920e+08
I(0) uncertainty (real space) i0_real_error9.2380e+06
Rg (reciprocal space) rg_reciprocal46.35
I(0) (reciprocal space) i0_reciprocal459000000.0000
Solution quality estimate total_estimate0.8421
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.1
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.758
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha69310000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.739; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.882; Smooth: 0.844

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)