8wvu

Cryo-EM structure of LGR4 in complex with Rspo1 and RNF43

Method: ELECTRON MICROSCOPY Dmax: 149.4 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 24–832 Not recorded R-spondin-1 × 1 (Q2MKA7) E3 ubiquitin-protein ligase RNF43 × 1 (Q68DV7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen PROPANE Resolution 3.61 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

R-spondin-1

Homo sapiens

UniProt Q2MKA7

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 B; UniProt 35–144 Not recorded Leucine-rich repeat-containing G-protein coupled receptor 4 × 1 (Q9BXB1) E3 ubiquitin-protein ligase RNF43 × 1 (Q68DV7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen PROPANE Resolution 3.61 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.

11 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RSPO1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–110; UniProt 35–144

E3 ubiquitin-protein ligase RNF43

Homo sapiens

UniProt Q68DV7

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 C; UniProt 44–198 Not recorded Leucine-rich repeat-containing G-protein coupled receptor 4 × 1 (Q9BXB1) R-spondin-1 × 1 (Q2MKA7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen PROPANE Resolution 3.61 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNF43_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–155; UniProt 44–198

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 8wvu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wvu
Deposition date deposition_date2023-10-24
Structure title titleCryo-EM structure of LGR4 in complex with Rspo1 and RNF43
Keywords keywordscomplex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.48
Radius of gyration Rg (electron density) rg_electron42.48
Forward intensity I(0) i0159386000.00
Molecular weight molecular_weight105630.0 kDa
Excluded volume excluded_volume133740 ų
Envelope volume envelope_volume197550 ų
Hydration-shell volume shell_volume42583 ų
Envelope diameter envelope_diameter158.0
Shell Rg shell_rg42.63
Envelope Rg envelope_rg41.51
Shape Rg shape_rg42.48
Total Rg total_rg42.47
Total atoms total_atoms7427
Residues n_residues972
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 dmax149.4
Rg (real space) rg_real41.92
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real1.5940e+08
I(0) uncertainty (real space) i0_real_error3.0790e+06
Rg (reciprocal space) rg_reciprocal41.48
I(0) (reciprocal space) i0_reciprocal159300000.0000
Solution quality estimate total_estimate0.8002
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.3
Skewness Skewness skewness0.609
Kurtosis Kurtosis kurtosis-0.199
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18240000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.656; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.750; Smooth: 0.679

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)