9z4o

Cryo-EM structure of human Wntless in its apo state

Method: ELECTRON MICROSCOPY Dmax: 103.4 Å Quality: GOOD

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

Protein wntless homolog

Homo sapiens

UniProt Q5T9L3

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 1–541 Not recorded No other associated polymer ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.63 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WLS_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–541; UniProt 1–541

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 9z4o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9z4o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9z4o
Deposition date deposition_date2025-11-10
Structure title titleCryo-EM structure of human Wntless in its apo state
Keywords keywordsWnt transporter, Wnt secretion, Wnt signaling, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.35
Radius of gyration Rg (electron density) rg_electron28.68
Forward intensity I(0) i043071600.00
Molecular weight molecular_weight55625.0 kDa
Excluded volume excluded_volume71424 ų
Envelope volume envelope_volume88639 ų
Hydration-shell volume shell_volume27522 ų
Envelope diameter envelope_diameter108.9
Shell Rg shell_rg33.80
Envelope Rg envelope_rg29.47
Shape Rg shape_rg28.64
Total Rg total_rg29.38
Total atoms total_atoms3920
Residues n_residues481
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 dmax103.4
Rg (real space) rg_real29.65
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real4.3070e+07
I(0) uncertainty (real space) i0_real_error6.8830e+05
Rg (reciprocal space) rg_reciprocal29.52
I(0) (reciprocal space) i0_reciprocal43070000.0000
Solution quality estimate total_estimate0.8094
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.597
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11110000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.615; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.722; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)