8wvw

Cryo-EM structure of LGR4 in state II

Method: ELECTRON MICROSCOPY Dmax: 140.4 Å Quality: REASONABLE

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

Leucine-rich repeat-containing G-protein coupled receptor 4

Homo sapiens

UniProt Q9BXB1

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 A; UniProt 24–832 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen PROPANE Resolution 3.53 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.

22 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LGR4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–832; UniProt 24–832

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 8wvw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wvw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wvw
Deposition date deposition_date2023-10-24
Structure title titleCryo-EM structure of LGR4 in state II
Keywords keywordsapp-form, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.04
Radius of gyration Rg (electron density) rg_electron44.82
Forward intensity I(0) i084807400.00
Molecular weight molecular_weight79299.0 kDa
Excluded volume excluded_volume101080 ų
Envelope volume envelope_volume156240 ų
Hydration-shell volume shell_volume31283 ų
Envelope diameter envelope_diameter152.0
Shell Rg shell_rg45.64
Envelope Rg envelope_rg43.18
Shape Rg shape_rg44.79
Total Rg total_rg44.94
Total atoms total_atoms5594
Residues n_residues722
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 dmax140.4
Rg (real space) rg_real44.52
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real8.4810e+07
I(0) uncertainty (real space) i0_real_error1.6490e+06
Rg (reciprocal space) rg_reciprocal44.04
I(0) (reciprocal space) i0_reciprocal84760000.0000
Solution quality estimate total_estimate0.7038
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.378
Kurtosis Kurtosis kurtosis-0.761
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4883000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.585; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.372; Smooth: 0.023

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)