9noy

Human TAS1R2 transmembrane domains from the TAS1R2-TM-G protein complex

Method: ELECTRON MICROSCOPY Dmax: 70.1 Å Quality: GOOD

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

Taste receptor type 1 member 2

Homo sapiens

UniProt Q8TE23

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–839 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TS1R2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 28–848; UniProt 19–839

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 9noy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9noy
Deposition date deposition_date2025-03-10
Structure title titleHuman TAS1R2 transmembrane domains from the TAS1R2-TM-G protein complex
Keywords keywordsSweet, taste, receptor, GPCR, TAS1R2, TAS1R3, T1R2, T1R3, membrane protein; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier21.11
Radius of gyration Rg (electron density) rg_electron20.09
Forward intensity I(0) i012203400.00
Molecular weight molecular_weight28931.0 kDa
Excluded volume excluded_volume37443 ų
Envelope volume envelope_volume44804 ų
Hydration-shell volume shell_volume19167 ų
Envelope diameter envelope_diameter70.8
Shell Rg shell_rg26.06
Envelope Rg envelope_rg20.48
Shape Rg shape_rg20.11
Total Rg total_rg21.01
Total atoms total_atoms2031
Residues n_residues257
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 dmax70.1
Rg (real space) rg_real21.14
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real1.2200e+07
I(0) uncertainty (real space) i0_real_error1.5650e+05
Rg (reciprocal space) rg_reciprocal21.14
I(0) (reciprocal space) i0_reciprocal12200000.0000
Solution quality estimate total_estimate0.8028
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.8
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.255
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2150000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)