8xfs

LGR4-RSPO2-ZNRF3 RING domain (1:2:2)

Method: ELECTRON MICROSCOPY Dmax: 150.6 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 31–821 Not recorded E3 ubiquitin-protein ligase ZNRF3 × 2 (Q9ULT6) nanobody Nb52 × 1 R-spondin-2 × 2 (Q8BFU0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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 1–791; UniProt 31–821

E3 ubiquitin-protein ligase ZNRF3

Homo sapiens

UniProt Q9ULT6

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 56–245 Chain E; UniProt 56–245 Not recorded Leucine-rich repeat-containing G-protein coupled receptor 4 × 1 (Q9BXB1) nanobody Nb52 × 1 R-spondin-2 × 2 (Q8BFU0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ZNRF3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–190; UniProt 56–245 Author chain E; PDBConstruct 1–190; UniProt 56–245

R-spondin-2

Homo sapiens

UniProt Q8BFU0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 41–141 Chain D; UniProt 41–141 Not recorded Leucine-rich repeat-containing G-protein coupled receptor 4 × 1 (Q9BXB1) E3 ubiquitin-protein ligase ZNRF3 × 2 (Q9ULT6) nanobody Nb52 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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

View Construct and Data Evidence
UniProt name RSPO2_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–101; UniProt 41–141 Author chain D; PDBConstruct 1–101; UniProt 41–141

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 8xfs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xfs
Deposition date deposition_date2023-12-14
Structure title titleLGR4-RSPO2-ZNRF3 RING domain (1:2:2)
Keywords keywordslgr4, znrf3 RING domain, 1:2:2, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.31
Radius of gyration Rg (electron density) rg_electron43.95
Forward intensity I(0) i0351956000.00
Molecular weight molecular_weight156290.0 kDa
Excluded volume excluded_volume196830 ų
Envelope volume envelope_volume281530 ų
Hydration-shell volume shell_volume56594 ų
Envelope diameter envelope_diameter159.6
Shell Rg shell_rg45.53
Envelope Rg envelope_rg43.61
Shape Rg shape_rg43.94
Total Rg total_rg44.07
Total atoms total_atoms10983
Residues n_residues1419
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 dmax150.6
Rg (real space) rg_real43.49
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real3.5200e+08
I(0) uncertainty (real space) i0_real_error6.0670e+06
Rg (reciprocal space) rg_reciprocal43.31
I(0) (reciprocal space) i0_reciprocal351900000.0000
Solution quality estimate total_estimate0.8674
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.2
Skewness Skewness skewness0.432
Kurtosis Kurtosis kurtosis-0.317
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25070000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.930; Smooth: 0.842

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)