8ctg

Extracellular architecture of an engineered canonical Wnt signaling ternary complex

Method: ELECTRON MICROSCOPY Dmax: 129.3 Å Quality: GOOD

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

Frizzled-8

Mus musculus

UniProt Q61091

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 28–150 Not recorded Protein Wnt-8 × 1 (P28026) Low-density lipoprotein receptor-related protein 6 × 1 (O75581) PAM PALMITOLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting before plunging Resolution 3.80 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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FZD8_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–123; UniProt 28–150

Protein Wnt-8

Xenopus laevis

UniProt P28026

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 22–329 Not recorded Frizzled-8 × 1 (Q61091) Low-density lipoprotein receptor-related protein 6 × 1 (O75581) PAM PALMITOLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting before plunging Resolution 3.80 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 WNT8_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–309; UniProt 22–329

Low-density lipoprotein receptor-related protein 6

Homo sapiens

UniProt O75581

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 20–629 Not recorded Frizzled-8 × 1 (Q61091) Protein Wnt-8 × 1 (P28026) PAM PALMITOLEIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3 s blotting before plunging Resolution 3.80 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.

27 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LRP6_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–612; UniProt 20–629

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 8ctg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ctg
Deposition date deposition_date2022-05-14
Structure title titleExtracellular architecture of an engineered canonical Wnt signaling ternary complex
Keywords keywordssignaling complex, beta-catenin, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.07
Radius of gyration Rg (electron density) rg_electron40.06
Forward intensity I(0) i0118950000.00
Molecular weight molecular_weight72268.0 kDa
Excluded volume excluded_volume83490 ų
Envelope volume envelope_volume164190 ų
Hydration-shell volume shell_volume35858 ų
Envelope diameter envelope_diameter131.5
Shell Rg shell_rg43.71
Envelope Rg envelope_rg38.43
Shape Rg shape_rg39.93
Total Rg total_rg40.61
Total atoms total_atoms5100
Residues n_residues1006
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 dmax129.3
Rg (real space) rg_real40.14
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real1.1900e+08
I(0) uncertainty (real space) i0_real_error1.9430e+06
Rg (reciprocal space) rg_reciprocal40.07
I(0) (reciprocal space) i0_reciprocal118900000.0000
Solution quality estimate total_estimate0.8640
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.0
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6946000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.906; Smooth: 0.486

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8ctgC01
Class class2 — Mainly Beta
Architecture architecture120 — 6 Propeller
Topology topology10 — Neuraminidase
Homologous superfamily homologous superfamily30 — TolB, C-terminal domain
Domain ID domain_id8ctgC02
Class class2 — Mainly Beta
Architecture architecture120 — 6 Propeller
Topology topology10 — Neuraminidase
Homologous superfamily homologous superfamily30 — TolB, C-terminal domain

8. Citations (1)

9. Files and Curves (10)