5wbs

Crystal structure of Frizzled-7 CRD with an inhibitor peptide Fz7-21

Method: X-RAY DIFFRACTION Dmax: 153.4 Å Quality: GOOD

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

Frizzled-7,inhibitor peptide Fz7-21

Homo sapiens

UniProt O75084

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 30–178 Chain B; UniProt 30–178 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;1-propanol 14% (v/v; cat. no. 09158; Fluka), 9% PEG5000 MME (cat. no. HR-2-615; Hampton Research), and 0.1 M MES at pH 6.9 (cat. no. HR2-243; Hampton Research) Resolution 2.88 Å R-free 0.244
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 30–178 Chain D; UniProt 30–178 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;1-propanol 14% (v/v; cat. no. 09158; Fluka), 9% PEG5000 MME (cat. no. HR-2-615; Hampton Research), and 0.1 M MES at pH 6.9 (cat. no. HR2-243; Hampton Research) Resolution 2.88 Å R-free 0.244
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 30–178 Chain F; UniProt 30–178 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;1-propanol 14% (v/v; cat. no. 09158; Fluka), 9% PEG5000 MME (cat. no. HR-2-615; Hampton Research), and 0.1 M MES at pH 6.9 (cat. no. HR2-243; Hampton Research) Resolution 2.88 Å R-free 0.244
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 30–178 Chain H; UniProt 30–178 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;1-propanol 14% (v/v; cat. no. 09158; Fluka), 9% PEG5000 MME (cat. no. HR-2-615; Hampton Research), and 0.1 M MES at pH 6.9 (cat. no. HR2-243; Hampton Research) Resolution 2.88 Å R-free 0.244

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FZD7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–149; UniProt 30–178 Author chain B; PDBConstruct 1–149; UniProt 30–178 Author chain C; PDBConstruct 1–149; UniProt 30–178 Author chain D; PDBConstruct 1–149; UniProt 30–178 Author chain E; PDBConstruct 1–149; UniProt 30–178 Author chain F; PDBConstruct 1–149; UniProt 30–178 Author chain G; PDBConstruct 1–149; UniProt 30–178 Author chain H; PDBConstruct 1–149; UniProt 30–178

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 5wbs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wbs
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5wbs
Deposition date deposition_date2017-06-29
Structure title titleCrystal structure of Frizzled-7 CRD with an inhibitor peptide Fz7-21
Keywords keywordsFrizzled, Wnt signaling, inhibitor, dimerization, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.64
Radius of gyration Rg (electron density) rg_electron43.68
Forward intensity I(0) i0226802000.00
Molecular weight molecular_weight119570.0 kDa
Excluded volume excluded_volume148160 ų
Envelope volume envelope_volume220260 ų
Hydration-shell volume shell_volume45736 ų
Envelope diameter envelope_diameter152.4
Shell Rg shell_rg43.68
Envelope Rg envelope_rg43.01
Shape Rg shape_rg43.68
Total Rg total_rg43.68
Total atoms total_atoms8359
Residues n_residues1057
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 dmax153.4
Rg (real space) rg_real43.76
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real2.2680e+08
I(0) uncertainty (real space) i0_real_error4.9780e+06
Rg (reciprocal space) rg_reciprocal43.64
I(0) (reciprocal space) i0_reciprocal226800000.0000
Solution quality estimate total_estimate0.7946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.4
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10900000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.800; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)