9on6

The pre-open state 2 structure of human P2X2 receptor channel in lipid nanodiscs with free ATP and sodium

Method: ELECTRON MICROSCOPY Dmax: 108.7 Å Quality: REASONABLE

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

P2X purinoceptor 2

Homo sapiens

UniProt Q9UBL9

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–471 Chain B; UniProt 1–471 Chain C; UniProt 1–471 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name P2RX2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–471; UniProt 1–471 Author chain B; PDBConstruct 1–471; UniProt 1–471 Author chain C; PDBConstruct 1–471; UniProt 1–471

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 9on6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9on6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9on6
Deposition date deposition_date2025-05-14
Structure title titleThe pre-open state 2 structure of human P2X2 receptor channel in lipid nanodiscs with free ATP and sodium
Keywords keywordsATP-gated ion channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.73
Radius of gyration Rg (electron density) rg_electron32.69
Forward intensity I(0) i0187027000.00
Molecular weight molecular_weight110740.0 kDa
Excluded volume excluded_volume139170 ų
Envelope volume envelope_volume184000 ų
Hydration-shell volume shell_volume47381 ų
Envelope diameter envelope_diameter114.5
Shell Rg shell_rg38.90
Envelope Rg envelope_rg33.16
Shape Rg shape_rg32.65
Total Rg total_rg33.33
Total atoms total_atoms7791
Residues n_residues969
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 dmax108.7
Rg (real space) rg_real32.77
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.8700e+08
I(0) uncertainty (real space) i0_real_error2.8920e+06
Rg (reciprocal space) rg_reciprocal32.75
I(0) (reciprocal space) i0_reciprocal187000000.0000
Solution quality estimate total_estimate0.6442
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.467
Kurtosis Kurtosis kurtosis0.010
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28050000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 0.049; Positv: 1.000; Valcen: 0.999; Smooth: 0.826

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)