9z32

The structure of short splice variant (Q9UBL9-2) of human P2X2 receptor channel in lipid nanodiscs with Mg-ATP

Method: ELECTRON MICROSCOPY Dmax: 111.5 Å Quality: GOOD

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

Isoform B of 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 1–404 Chain B; UniProt 1–404 Chain C; UniProt 1–404 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 2.83 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.

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 Q9UBL9-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–404; UniProt 1–404 Author chain B; PDBConstruct 1–404; UniProt 1–404 Author chain C; PDBConstruct 1–404; UniProt 1–404

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 9z32

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9z32
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9z32
Deposition date deposition_date2025-11-05
Structure title titleThe structure of short splice variant (Q9UBL9-2) of human P2X2 receptor channel in lipid nanodiscs with Mg-ATP
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_guinier32.79
Radius of gyration Rg (electron density) rg_electron32.92
Forward intensity I(0) i0188453000.00
Molecular weight molecular_weight111410.0 kDa
Excluded volume excluded_volume140040 ų
Envelope volume envelope_volume185230 ų
Hydration-shell volume shell_volume47406 ų
Envelope diameter envelope_diameter118.6
Shell Rg shell_rg39.07
Envelope Rg envelope_rg33.59
Shape Rg shape_rg32.87
Total Rg total_rg33.58
Total atoms total_atoms7836
Residues n_residues972
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 dmax111.5
Rg (real space) rg_real32.86
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.8850e+08
I(0) uncertainty (real space) i0_real_error3.2590e+06
Rg (reciprocal space) rg_reciprocal32.83
I(0) (reciprocal space) i0_reciprocal188400000.0000
Solution quality estimate total_estimate0.8577
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.5
Skewness Skewness skewness0.498
Kurtosis Kurtosis kurtosis0.052
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29190000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)