9c5y

Structure of the amino-terminal domain of kainate receptor GluK2 in the apo state

Method: ELECTRON MICROSCOPY Dmax: 147.9 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 Protein homooligomer Homooligomer Protein × 4 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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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 9c5y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c5y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c5y
Deposition date deposition_date2024-06-07
Structure title titleStructure of the amino-terminal domain of kainate receptor GluK2 in the apo state
Keywords keywordsC1, membrane, glycosylation, glutamate, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.64
Radius of gyration Rg (electron density) rg_electron45.62
Forward intensity I(0) i0436265000.00
Molecular weight molecular_weight174790.0 kDa
Excluded volume excluded_volume219630 ų
Envelope volume envelope_volume292630 ų
Hydration-shell volume shell_volume54660 ų
Envelope diameter envelope_diameter150.7
Shell Rg shell_rg48.29
Envelope Rg envelope_rg44.97
Shape Rg shape_rg45.61
Total Rg total_rg45.76
Total atoms total_atoms12302
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 dmax147.9
Rg (real space) rg_real45.91
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real4.3630e+08
I(0) uncertainty (real space) i0_real_error7.9660e+06
Rg (reciprocal space) rg_reciprocal45.65
I(0) (reciprocal space) i0_reciprocal436100000.0000
Solution quality estimate total_estimate0.8223
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.0
Skewness Skewness skewness0.351
Kurtosis Kurtosis kurtosis-0.763
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62260000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.793; Smooth: 0.432

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)