3cbz

The Dvl2 PDZ Domain in Complex with the N2 Inhibitory Peptide

Method: X-RAY DIFFRACTION Dmax: 62.6 Å Quality: REASONABLE

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

Dishevelled-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 264–354 Fragment:PDZ domain (UNP residues 264-354) Mutation:C341S PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;292 K;0.1 M HEPES, 0.8 M sodium phosphate, 0.8 M Potassium phosphate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 1.38 Å R-free 0.166

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 5–95; UniProt 264–354

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 3cbz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3cbz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3cbz
Deposition date deposition_date2008-02-23
Structure title titleThe Dvl2 PDZ Domain in Complex with the N2 Inhibitory Peptide
Keywords keywords;PDZ DOMAIN, PHAGE DERIVED HIGH AFFINITY LIGAND, Cytoplasm, Developmental protein, Phosphoprotein, Wnt signaling pathway, SIGNALING PROTEIN, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.62
Radius of gyration Rg (electron density) rg_electron14.33
Forward intensity I(0) i02887020.00
Molecular weight molecular_weight11291.0 kDa
Excluded volume excluded_volume13944 ų
Envelope volume envelope_volume17047 ų
Hydration-shell volume shell_volume10766 ų
Envelope diameter envelope_diameter62.3
Shell Rg shell_rg19.57
Envelope Rg envelope_rg15.32
Shape Rg shape_rg14.37
Total Rg total_rg15.38
Total atoms total_atoms787
Residues n_residues104
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 dmax62.6
Rg (real space) rg_real15.71
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real2.8870e+06
I(0) uncertainty (real space) i0_real_error3.7830e+04
Rg (reciprocal space) rg_reciprocal15.70
I(0) (reciprocal space) i0_reciprocal2887000.0000
Solution quality estimate total_estimate0.7483
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.671
Kurtosis Kurtosis kurtosis0.891
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha463900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.345; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.706; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3cbza1
Class classb — All beta proteins
Fold Fold foldb.36 — PDZ domain-like
Superfamily Superfamily superfamilyb.36.1 — PDZ domain-like
Family Family familyb.36.1.1 — PDZ domain
Domain ID domain_idd3cbza2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id3cbzA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)