9uta

The transmembrane domains of human sweet taste receptor TAS1R2 and TAS1R3 in the apo state

Method: ELECTRON MICROSCOPY Dmax: 102.7 Å Quality: GOOD

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

Taste receptor type 1 member 2,Engineered red fluorescent protein mScarlet3

Discosoma sp. (Sea anemone)

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 26–839 Not recorded Taste receptor type 1 member 3,mNeonGreen × 1 (Q7RTX0,A0A1S4NYF2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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 30–843; UniProt 26–839

Taste receptor type 1 member 3,mNeonGreen

Branchiostoma lanceolatum

UniProt A0A1S4NYF2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 26–260 Not recorded Taste receptor type 1 member 2,Engineered red fluorescent protein mScarlet3 × 1 (Q8TE23) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1S4NYF2_BRALA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 876–1110; UniProt 26–260

Taste receptor type 1 member 3,mNeonGreen

Branchiostoma lanceolatum

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 21–852 Not recorded Taste receptor type 1 member 2,Engineered red fluorescent protein mScarlet3 × 1 (Q8TE23) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.77 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 2
Chains and sequence ranges Author chain B; PDBConstruct 29–860; UniProt 21–852

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 9uta

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9uta
Deposition date deposition_date2025-05-03
Structure title titleThe transmembrane domains of human sweet taste receptor TAS1R2 and TAS1R3 in the apo state
Keywords keywordsGPCR, Taste, Tas1R2, Tas1R3, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.26
Radius of gyration Rg (electron density) rg_electron30.00
Forward intensity I(0) i062683800.00
Molecular weight molecular_weight66899.0 kDa
Excluded volume excluded_volume85757 ų
Envelope volume envelope_volume114810 ų
Hydration-shell volume shell_volume32592 ų
Envelope diameter envelope_diameter104.9
Shell Rg shell_rg36.19
Envelope Rg envelope_rg29.88
Shape Rg shape_rg30.02
Total Rg total_rg30.59
Total atoms total_atoms4701
Residues n_residues602
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 dmax102.7
Rg (real space) rg_real31.28
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real6.2680e+07
I(0) uncertainty (real space) i0_real_error1.0270e+06
Rg (reciprocal space) rg_reciprocal31.27
I(0) (reciprocal space) i0_reciprocal62680000.0000
Solution quality estimate total_estimate0.8917
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.3
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5778000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)