6ndz

Designed repeat protein in complex with Fz8

Method: X-RAY DIFFRACTION Dmax: 109.7 Å Quality: EXCELLENT

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 32–150 Mutation:N49Q Designed repeat binding protein × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 4 ACT ACETATE ION × 3 ACY ACETIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M ammonium acetate, 0.1 M HEPE, pH 7.5 and 55% MPD Resolution 2.26 Å R-free 0.238
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 32–150 Mutation:N49Q Designed repeat binding protein × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M ammonium acetate, 0.1 M HEPE, pH 7.5 and 55% MPD Resolution 2.26 Å R-free 0.238
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 32–150 Mutation:N49Q Designed repeat binding protein × 1 ACY ACETIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M ammonium acetate, 0.1 M HEPE, pH 7.5 and 55% MPD Resolution 2.26 Å R-free 0.238

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 9 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 1–119; UniProt 32–150 Author chain C; PDBConstruct 1–119; UniProt 32–150 Author chain E; PDBConstruct 1–119; UniProt 32–150

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 6ndz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ndz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ndz
Deposition date deposition_date2018-12-14
Structure title titleDesigned repeat protein in complex with Fz8
Keywords keywordsFrizzled, Designed protein, BIOSYNTHETIC PROTEIN, BIOSYNTHETIC PROTEIN-SIGNALING PROTEIN complex; BIOSYNTHETIC PROTEIN/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.50
Radius of gyration Rg (electron density) rg_electron33.86
Forward intensity I(0) i0165119000.00
Molecular weight molecular_weight101060.0 kDa
Excluded volume excluded_volume126010 ų
Envelope volume envelope_volume165640 ų
Hydration-shell volume shell_volume41356 ų
Envelope diameter envelope_diameter114.4
Shell Rg shell_rg39.96
Envelope Rg envelope_rg33.26
Shape Rg shape_rg33.85
Total Rg total_rg34.37
Total atoms total_atoms7067
Residues n_residues931
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 dmax109.7
Rg (real space) rg_real34.44
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.6510e+08
I(0) uncertainty (real space) i0_real_error2.7630e+06
Rg (reciprocal space) rg_reciprocal34.48
I(0) (reciprocal space) i0_reciprocal165100000.0000
Solution quality estimate total_estimate0.9085
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.641
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13490000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.941

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6ndzB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain
Domain ID domain_id6ndzD00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain
Domain ID domain_id6ndzF00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain

8. Citations (1)

9. Files and Curves (10)