9ggg

Cryo-EM structure of Thromboxane A2 receptor-miniGq Protein Complex bound to I-BOP

Method: ELECTRON MICROSCOPY Dmax: 122.9 Å Quality: EXCELLENT

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

Thromboxane A2 receptor

Homo sapiens

UniProt P21731

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 1–343 Not recorded Engineered miniGq × 1 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) Antibody fragment scFv16 × 1 A1IK0 (~{Z})-7-[(1~{S},2~{R},3~{R},4~{R})-3-[(~{E},3~{R})-4-(4-iodanylphenoxy)-3-oxidanyl-but-1-enyl]-7-oxabicyclo[2.2.1]heptan-2-yl]hept-5-enoic acid × 1 CLR CHOLESTEROL × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.25 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TA2R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–343; UniProt 1–343

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 Thromboxane A2 receptor × 1 (P21731) Engineered miniGq × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Antibody fragment scFv16 × 1 A1IK0 (~{Z})-7-[(1~{S},2~{R},3~{R},4~{R})-3-[(~{E},3~{R})-4-(4-iodanylphenoxy)-3-oxidanyl-but-1-enyl]-7-oxabicyclo[2.2.1]heptan-2-yl]hept-5-enoic acid × 1 CLR CHOLESTEROL × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.25 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 3
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 Thromboxane A2 receptor × 1 (P21731) Engineered miniGq × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Antibody fragment scFv16 × 1 A1IK0 (~{Z})-7-[(1~{S},2~{R},3~{R},4~{R})-3-[(~{E},3~{R})-4-(4-iodanylphenoxy)-3-oxidanyl-but-1-enyl]-7-oxabicyclo[2.2.1]heptan-2-yl]hept-5-enoic acid × 1 CLR CHOLESTEROL × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.25 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 4
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 9ggg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ggg
Deposition date deposition_date2024-08-13
Structure title titleCryo-EM structure of Thromboxane A2 receptor-miniGq Protein Complex bound to I-BOP
Keywords keywordsSingle particle cryo-EM, GPCR, G-proteins, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.09
Radius of gyration Rg (electron density) rg_electron37.86
Forward intensity I(0) i0437956000.00
Molecular weight molecular_weight114390.0 kDa
Excluded volume excluded_volume111120 ų
Envelope volume envelope_volume208420 ų
Hydration-shell volume shell_volume46773 ų
Envelope diameter envelope_diameter123.1
Shell Rg shell_rg42.68
Envelope Rg envelope_rg37.65
Shape Rg shape_rg37.88
Total Rg total_rg38.05
Total atoms total_atoms8656
Residues n_residues1159
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 dmax122.9
Rg (real space) rg_real38.01
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real4.3800e+08
I(0) uncertainty (real space) i0_real_error7.8520e+06
Rg (reciprocal space) rg_reciprocal38.07
I(0) (reciprocal space) i0_reciprocal438000000.0000
Solution quality estimate total_estimate0.9013
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.7
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.697
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39910000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)