8z67

Cryo-EM structure of the hGPR68-Gs complex in pH6.8

Method: ELECTRON MICROSCOPY Dmax: 69.8 Å Quality: GOOD

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

G-protein coupled receptor 4

Homo sapiens

UniProt P46093

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain R; UniProt 1–362 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 GPR4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–362; UniProt 1–362

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 8z67

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8z67
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8z67
Deposition date deposition_date2024-04-18
Structure title titleCryo-EM structure of the hGPR68-Gs complex in pH6.8
Keywords keywordspH6.8, hGPR68, Gs, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier21.51
Radius of gyration Rg (electron density) rg_electron20.33
Forward intensity I(0) i016056200.00
Molecular weight molecular_weight32541.0 kDa
Excluded volume excluded_volume41639 ų
Envelope volume envelope_volume47537 ų
Hydration-shell volume shell_volume19969 ų
Envelope diameter envelope_diameter72.2
Shell Rg shell_rg26.59
Envelope Rg envelope_rg20.83
Shape Rg shape_rg20.34
Total Rg total_rg21.23
Total atoms total_atoms2304
Residues n_residues297
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 dmax69.8
Rg (real space) rg_real21.56
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.6060e+07
I(0) uncertainty (real space) i0_real_error2.0050e+05
Rg (reciprocal space) rg_reciprocal21.55
I(0) (reciprocal space) i0_reciprocal16060000.0000
Solution quality estimate total_estimate0.8065
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2358000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.839; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)