9n4q

Composite map for GluK2-2xNeto2 in the apo state

Method: ELECTRON MICROSCOPY Dmax: 193.4 Å Quality: REASONABLE

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 Heteromer Protein × 6 其他Polymer 17 PDB declaration: hexameric(6) 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 Neuropilin and tolloid-like protein 2 × 2 (C6K2K4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 ;beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 15 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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

Neuropilin and tolloid-like protein 2

Rattus norvegicus

UniProt C6K2K4

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 Heteromer Protein × 6 其他Polymer 17 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–525 Chain F; UniProt 1–525 Not recorded Glutamate receptor ionotropic, kainate 2 × 4 (P42260) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 ;beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 15 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NETO2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–525; UniProt 1–525 Author chain F; PDBConstruct 1–525; UniProt 1–525

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 9n4q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n4q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n4q
Deposition date deposition_date2025-02-03
Structure title titleComposite map for GluK2-2xNeto2 in the apo state
Keywords keywordsKainate receptor, GluK2, Ion Channel, Neto2, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.96
Radius of gyration Rg (electron density) rg_electron63.53
Forward intensity I(0) i02948870000.00
Molecular weight molecular_weight474510.0 kDa
Excluded volume excluded_volume601060 ų
Envelope volume envelope_volume946110 ų
Hydration-shell volume shell_volume128710 ų
Envelope diameter envelope_diameter218.4
Shell Rg shell_rg62.58
Envelope Rg envelope_rg61.25
Shape Rg shape_rg63.51
Total Rg total_rg63.57
Total atoms total_atoms33333
Residues n_residues3998
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 dmax193.4
Rg (real space) rg_real63.06
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real2.9480e+09
I(0) uncertainty (real space) i0_real_error5.5720e+07
Rg (reciprocal space) rg_reciprocal62.83
I(0) (reciprocal space) i0_reciprocal2947000000.0000
Solution quality estimate total_estimate0.6179
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary77.4
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.183
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha229400000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 0.999; Sysdev: 0.004; Positv: 1.000; Valcen: 0.987; Smooth: 0.206

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)