8wwr

Crystal structure of apo human dishevelled 2 (Dvl2) PDZ domain

Method: X-RAY DIFFRACTION Dmax: 48.8 Å Quality: GOOD

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

Segment polarity protein dishevelled homolog DVL-2

Homo sapiens

UniProt O14641

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 261–354 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1M Tri-sodium citrate, pH 5.6 20% (v/v) Isopropanol 20%(w/v) PEG4000 Resolution 1.75 Å R-free 0.253

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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DVL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–95; UniProt 261–354

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 8wwr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wwr
Deposition date deposition_date2023-10-26
最后修订 last_revision2024-05-29
Structure title titleCrystal structure of apo human dishevelled 2 (Dvl2) PDZ domain
Keywords keywordsWnt signaling, 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_guinier13.88
Radius of gyration Rg (electron density) rg_electron12.20
Forward intensity I(0) i01707600.00
Molecular weight molecular_weight8902.0 kDa
Excluded volume excluded_volume11246 ų
Envelope volume envelope_volume13056 ų
Hydration-shell volume shell_volume9420 ų
Envelope diameter envelope_diameter43.0
Shell Rg shell_rg17.55
Envelope Rg envelope_rg12.51
Shape Rg shape_rg12.16
Total Rg total_rg13.69
Total atoms total_atoms1241
Residues n_residues87
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 dmax48.8
Rg (real space) rg_real13.77
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real1.7080e+06
I(0) uncertainty (real space) i0_real_error1.9080e+04
Rg (reciprocal space) rg_reciprocal13.78
I(0) (reciprocal space) i0_reciprocal1708000.0000
Solution quality estimate total_estimate0.7624
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.5
Skewness Skewness skewness0.045
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha260900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.636; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; 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)