5un5

Frizzled-8 complex with designed surrogate Wnt agonist, crystal form 1

Method: X-RAY DIFFRACTION Dmax: 103.3 Å Quality: REASONABLE

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

Frizzled-8

Homo sapiens

UniProt Q9H461

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 28–150 Chain B; UniProt 28–150 Fragment:UNP residues 28-150 Designed Wnt agonist B12 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;295 K;42-49% PEG 400, 0.1 M Tris pH 7.8-8.2, 0.2 M NaCl Resolution 2.99 Å R-free 0.250

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FZD8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–123; UniProt 28–150 Author chain B; PDBConstruct 1–123; UniProt 28–150

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 5un5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5un5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5un5
Deposition date deposition_date2017-01-30
Structure title titleFrizzled-8 complex with designed surrogate Wnt agonist, crystal form 1
Keywords keywordsSIGNALING PROTEIN, SIGNALING PROTEIN-De Novo Protein complex; SIGNALING PROTEIN/De Novo Protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.31
Radius of gyration Rg (electron density) rg_electron31.81
Forward intensity I(0) i034715600.00
Molecular weight molecular_weight46192.0 kDa
Excluded volume excluded_volume57888 ų
Envelope volume envelope_volume79320 ų
Hydration-shell volume shell_volume22799 ų
Envelope diameter envelope_diameter110.2
Shell Rg shell_rg35.46
Envelope Rg envelope_rg31.42
Shape Rg shape_rg31.82
Total Rg total_rg32.14
Total atoms total_atoms3230
Residues n_residues417
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 dmax103.3
Rg (real space) rg_real32.68
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real3.4720e+07
I(0) uncertainty (real space) i0_real_error5.9420e+05
Rg (reciprocal space) rg_reciprocal32.53
I(0) (reciprocal space) i0_reciprocal34710000.0000
Solution quality estimate total_estimate0.5961
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.392
Kurtosis Kurtosis kurtosis-0.805
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3822000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.744; Stabil: 1.000; Sysdev: 0.096; Positv: 1.000; Valcen: 0.534; Smooth: 0.692

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5un5A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2000 — Frizzled cysteine-rich domain
Homologous superfamily homologous superfamily10 — Frizzled cysteine-rich domain
Domain ID domain_id5un5B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2000 — Frizzled cysteine-rich domain
Homologous superfamily homologous superfamily10 — Frizzled cysteine-rich domain

8. Citations (1)

9. Files and Curves (10)