9osf

The intact LBD state of GluK2/K5 with 5-iodowillardiine and kynurenic acid sodium salt

Method: ELECTRON MICROSCOPY Dmax: 209.9 Å Quality: GOOD

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

Glutamate receptor ionotropic, kainate 5,Green fluorescent protein chimera

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–238 Chain C; UniProt 2–238 Not recorded Glutamate receptor ionotropic, kainate 2 × 2 (P42260) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris, 300 mM NaCl, 0.35 mM DDM, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.83 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 852–1088; UniProt 2–238 Author chain C; PDBConstruct 852–1088; UniProt 2–238

Glutamate receptor ionotropic, kainate 5,Green fluorescent protein chimera

Aequorea victoria

UniProt Q63273

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–827 Chain C; UniProt 1–827 Not recorded Glutamate receptor ionotropic, kainate 2 × 2 (P42260) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris, 300 mM NaCl, 0.35 mM DDM, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.83 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.

8 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIK5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–827; UniProt 1–827 Author chain C; PDBConstruct 1–827; UniProt 1–827

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 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–908 Chain D; UniProt 1–908 Not recorded Glutamate receptor ionotropic, kainate 5,Green fluorescent protein chimera × 2 (Q63273,P42212) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris, 300 mM NaCl, 0.35 mM DDM, pH 8.0 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.83 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 2
Chains and sequence ranges Author chain B; 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 9osf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9osf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9osf
Deposition date deposition_date2025-05-24
Structure title titleThe intact LBD state of GluK2/K5 with 5-iodowillardiine and kynurenic acid sodium salt
Keywords keywordsKainate receptor, ionotropic glutamate receptor, membrane protein, ligand-gated ion channel, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.12
Radius of gyration Rg (electron density) rg_electron60.79
Forward intensity I(0) i01535640000.00
Molecular weight molecular_weight338070.0 kDa
Excluded volume excluded_volume426850 ų
Envelope volume envelope_volume670280 ų
Hydration-shell volume shell_volume93625 ų
Envelope diameter envelope_diameter204.9
Shell Rg shell_rg61.40
Envelope Rg envelope_rg59.19
Shape Rg shape_rg60.80
Total Rg total_rg60.75
Total atoms total_atoms23794
Residues n_residues3004
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 dmax209.9
Rg (real space) rg_real60.16
Rg uncertainty (real space) rg_real_error2.46
I(0) (real space) i0_real1.5360e+09
I(0) uncertainty (real space) i0_real_error3.0230e+07
Rg (reciprocal space) rg_reciprocal60.06
I(0) (reciprocal space) i0_reciprocal1535000000.0000
Solution quality estimate total_estimate0.8646
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.7
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha114400000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.713

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)