6ne4

Designed repeat protein specifically in complex with Fz7CRD

Method: X-RAY DIFFRACTION Dmax: 69.6 Å Quality: GOOD

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

Frizzled-7

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 46–163 Not recorded Designed repeat binding protein × 1 SO4 SULFATE ION × 14 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M Na2HPO4, citric acid, pH 4.2 and 2M Ammonium sulfate Resolution 1.65 Å R-free 0.186

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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FZD7_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–118; UniProt 46–163

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 6ne4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ne4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ne4
Deposition date deposition_date2018-12-16
Structure title titleDesigned repeat protein specifically in complex with Fz7CRD
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_guinier21.27
Radius of gyration Rg (electron density) rg_electron20.44
Forward intensity I(0) i024546600.00
Molecular weight molecular_weight34940.0 kDa
Excluded volume excluded_volume42545 ų
Envelope volume envelope_volume50216 ų
Hydration-shell volume shell_volume20727 ų
Envelope diameter envelope_diameter71.8
Shell Rg shell_rg26.76
Envelope Rg envelope_rg20.75
Shape Rg shape_rg20.40
Total Rg total_rg21.32
Total atoms total_atoms2422
Residues n_residues312
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 dmax69.6
Rg (real space) rg_real21.20
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.4550e+07
I(0) uncertainty (real space) i0_real_error2.9950e+05
Rg (reciprocal space) rg_reciprocal21.22
I(0) (reciprocal space) i0_reciprocal24550000.0000
Solution quality estimate total_estimate0.8954
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6541000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6ne4B00
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)