9p90

Avian TRPM8 (Parus major) desensitized, fully-swapped, ligand-free structure resolved in cell vesicles using cryo-EM

Method: ELECTRON MICROSCOPY Dmax: 165.4 Å Quality: GOOD

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

Transient receptor potential cation channel subfamily M member 8

Parus major

UniProt A0A5S8WF66

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 6–1098 Chain B; UniProt 6–1098 Chain C; UniProt 6–1098 Chain D; UniProt 6–1098 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5S8WF66_PARMJ
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–1101; UniProt 6–1098 Author chain B; PDBConstruct 9–1101; UniProt 6–1098 Author chain C; PDBConstruct 9–1101; UniProt 6–1098 Author chain D; PDBConstruct 9–1101; UniProt 6–1098

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 9p90

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9p90
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9p90
Deposition date deposition_date2025-06-23
Structure title titleAvian TRPM8 (Parus major) desensitized, fully-swapped, ligand-free structure resolved in cell vesicles using cryo-EM
Keywords keywordsTRPM8, transient receptor potential melastatin 8, MEMBRANE PROTEIN, Parus major; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.93
Radius of gyration Rg (electron density) rg_electron52.34
Forward intensity I(0) i02453200000.00
Molecular weight molecular_weight436680.0 kDa
Excluded volume excluded_volume554340 ų
Envelope volume envelope_volume818330 ų
Hydration-shell volume shell_volume125800 ų
Envelope diameter envelope_diameter167.3
Shell Rg shell_rg60.39
Envelope Rg envelope_rg50.09
Shape Rg shape_rg52.36
Total Rg total_rg52.53
Total atoms total_atoms60860
Residues n_residues3884
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 dmax165.4
Rg (real space) rg_real52.62
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real2.4530e+09
I(0) uncertainty (real space) i0_real_error5.1770e+07
Rg (reciprocal space) rg_reciprocal53.19
I(0) (reciprocal space) i0_reciprocal2455000000.0000
Solution quality estimate total_estimate0.8888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.7
Skewness Skewness skewness0.030
Kurtosis Kurtosis kurtosis-0.537
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha263300000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)