8tzs

Structure of human WLS

Method: ELECTRON MICROSCOPY Dmax: 103.9 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 cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.84 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 8tzs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tzs
Deposition date deposition_date2023-08-27
Structure title titleStructure of human WLS
Keywords keywordsMEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.31
Radius of gyration Rg (electron density) rg_electron29.53
Forward intensity I(0) i043344700.00
Molecular weight molecular_weight55559.0 kDa
Excluded volume excluded_volume71233 ų
Envelope volume envelope_volume91361 ų
Hydration-shell volume shell_volume27874 ų
Envelope diameter envelope_diameter109.3
Shell Rg shell_rg34.29
Envelope Rg envelope_rg29.86
Shape Rg shape_rg29.50
Total Rg total_rg30.15
Total atoms total_atoms3914
Residues n_residues480
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 dmax103.9
Rg (real space) rg_real30.62
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real4.3340e+07
I(0) uncertainty (real space) i0_real_error6.7070e+05
Rg (reciprocal space) rg_reciprocal30.49
I(0) (reciprocal space) i0_reciprocal43340000.0000
Solution quality estimate total_estimate0.8166
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.0
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis-0.389
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha11220000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.670; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.673; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)