9m2o

Cryo-EM structure of the putrescine-bound zTAAR13d-Gs complex

Method: ELECTRON MICROSCOPY Dmax: 123.3 Å Quality: GOOD

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

Trace amine-associated receptor 13d

Homo sapiens

UniProt Q5QNQ1

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 1–341 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Nb35 × 1 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 PUT 1,4-DIAMINOBUTANE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.59 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5QNQ1_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–341; UniProt 1–341

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Homo sapiens

UniProt P62873

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–340 Not recorded Trace amine-associated receptor 13d × 1 (Q5QNQ1) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Nb35 × 1 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 PUT 1,4-DIAMINOBUTANE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.59 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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Homo sapiens

UniProt P59768

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–71 Not recorded Trace amine-associated receptor 13d × 1 (Q5QNQ1) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Nb35 × 1 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 PUT 1,4-DIAMINOBUTANE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.59 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.

1233 other PDB entries and 1236 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–71; UniProt 1–71

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 9m2o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m2o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9m2o
Deposition date deposition_date2025-02-28
Structure title titleCryo-EM structure of the putrescine-bound zTAAR13d-Gs complex
Keywords keywordsGPCR, combinatorial coding, zebrafish, TAAR13 family, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.61
Radius of gyration Rg (electron density) rg_electron35.71
Forward intensity I(0) i0221444000.00
Molecular weight molecular_weight120080.0 kDa
Excluded volume excluded_volume150250 ų
Envelope volume envelope_volume189420 ų
Hydration-shell volume shell_volume45601 ų
Envelope diameter envelope_diameter132.2
Shell Rg shell_rg40.45
Envelope Rg envelope_rg36.14
Shape Rg shape_rg35.68
Total Rg total_rg36.09
Total atoms total_atoms8434
Residues n_residues1071
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 dmax123.3
Rg (real space) rg_real35.85
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real2.2140e+08
I(0) uncertainty (real space) i0_real_error3.8290e+06
Rg (reciprocal space) rg_reciprocal35.70
I(0) (reciprocal space) i0_reciprocal221400000.0000
Solution quality estimate total_estimate0.8408
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.560
Kurtosis Kurtosis kurtosis-0.092
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44910000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.765; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.740

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)