9nov

Human sweet taste receptor (TAS1R2 + TAS1R3) VFT domains bound to sucralose

Method: ELECTRON MICROSCOPY Dmax: 97.8 Å Quality: EXCELLENT

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

Taste receptor type 1 member 3

Homo sapiens

UniProt Q7RTX0

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 × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 21–521 Not recorded Taste receptor type 1 member 2 × 1 (Q8TE23) 4-chloro-4-deoxy-alpha-D-galactopyranose-(1-2)-1,6-dichloro-1,6-dideoxy-beta-D-fructofuranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TS1R3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 28–528; UniProt 21–521

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 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–518 Not recorded Taste receptor type 1 member 3 × 1 (Q7RTX0) 4-chloro-4-deoxy-alpha-D-galactopyranose-(1-2)-1,6-dichloro-1,6-dideoxy-beta-D-fructofuranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2
Chains and sequence ranges Author chain A; PDBConstruct 28–527; UniProt 19–518

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 9nov

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9nov
Deposition date deposition_date2025-03-10
Structure title titleHuman sweet taste receptor (TAS1R2 + TAS1R3) VFT domains bound to sucralose
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_guinier31.02
Radius of gyration Rg (electron density) rg_electron29.82
Forward intensity I(0) i0185019000.00
Molecular weight molecular_weight108840.0 kDa
Excluded volume excluded_volume136460 ų
Envelope volume envelope_volume169410 ų
Hydration-shell volume shell_volume45253 ų
Envelope diameter envelope_diameter107.1
Shell Rg shell_rg38.50
Envelope Rg envelope_rg29.90
Shape Rg shape_rg29.80
Total Rg total_rg30.67
Total atoms total_atoms7647
Residues n_residues936
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 dmax97.8
Rg (real space) rg_real30.85
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.8500e+08
I(0) uncertainty (real space) i0_real_error2.6430e+06
Rg (reciprocal space) rg_reciprocal30.93
I(0) (reciprocal space) i0_reciprocal185000000.0000
Solution quality estimate total_estimate0.9009
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.5
Skewness Skewness skewness0.159
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76970000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)