9jqz

Structural Insights into Selective Antagonism Grapiprant and EP4 Prostaglandin Receptor

Method: ELECTRON MICROSCOPY Dmax: 135.4 Å Quality: REASONABLE

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

GFP-like fluorescent chromoprotein,Prostaglandin E2 receptor EP4 subtype

Homo sapiens

UniProt P35408

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 2–366 Mutation:T228A,N232Q,A287L,G331R,N402Q Heavy chain of Fab fragment × 1 Light chain of Fab fragment × 1 A1ECR Grapiprant × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.65 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PE2R4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 227–549; UniProt 2–366

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 9jqz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jqz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9jqz
Deposition date deposition_date2024-09-28
Structure title titleStructural Insights into Selective Antagonism Grapiprant and EP4 Prostaglandin Receptor
Keywords keywordsGPCR, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE PROTEIN-IMMUNE SYSTEM complex; MEMBRANE PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.82
Radius of gyration Rg (electron density) rg_electron37.46
Forward intensity I(0) i0166628000.00
Molecular weight molecular_weight70809.0 kDa
Excluded volume excluded_volume69283 ų
Envelope volume envelope_volume131350 ų
Hydration-shell volume shell_volume32914 ų
Envelope diameter envelope_diameter138.3
Shell Rg shell_rg37.72
Envelope Rg envelope_rg38.30
Shape Rg shape_rg37.46
Total Rg total_rg37.49
Total atoms total_atoms5367
Residues n_residues682
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 dmax135.4
Rg (real space) rg_real37.54
Rg uncertainty (real space) rg_real_error2.21
I(0) (real space) i0_real1.6660e+08
I(0) uncertainty (real space) i0_real_error3.5730e+06
Rg (reciprocal space) rg_reciprocal37.09
I(0) (reciprocal space) i0_reciprocal166600000.0000
Solution quality estimate total_estimate0.7227
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.5
Skewness Skewness skewness0.699
Kurtosis Kurtosis kurtosis-0.154
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9035000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.470; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.233; Smooth: 0.749

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)