4wip

DIX domain of human Dvl2

Method: X-RAY DIFFRACTION Dmax: 82.9 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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 12–106 Chain B; UniProt 12–106 Chain C; UniProt 12–106 Fragment:UNP residues 13-105 Mutation:Y27D 1PE PENTAETHYLENE GLYCOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;292 K;grew in PEG400 (cryo condition) over night Resolution 2.69 Å R-free 0.248

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 2–96; UniProt 12–106 Author chain B; PDBConstruct 2–96; UniProt 12–106 Author chain C; PDBConstruct 2–96; UniProt 12–106

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 4wip

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4wip
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4wip
Deposition date deposition_date2014-09-26
Structure title titleDIX domain of human Dvl2
Keywords keywordspolymer signaling ubiquitin-like, 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_guinier23.59
Radius of gyration Rg (electron density) rg_electron22.75
Forward intensity I(0) i013431100.00
Molecular weight molecular_weight28131.0 kDa
Excluded volume excluded_volume35531 ų
Envelope volume envelope_volume45187 ų
Hydration-shell volume shell_volume18068 ų
Envelope diameter envelope_diameter84.6
Shell Rg shell_rg27.58
Envelope Rg envelope_rg22.82
Shape Rg shape_rg22.70
Total Rg total_rg23.64
Total atoms total_atoms1981
Residues n_residues243
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 dmax82.9
Rg (real space) rg_real23.78
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.3430e+07
I(0) uncertainty (real space) i0_real_error2.2290e+05
Rg (reciprocal space) rg_reciprocal23.74
I(0) (reciprocal space) i0_reciprocal13430000.0000
Solution quality estimate total_estimate0.8297
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.519
Kurtosis Kurtosis kurtosis-0.278
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3676000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.697; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.704; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4wipa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.0 — automated matches
Domain ID domain_idd4wipb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.0 — automated matches
Domain ID domain_idd4wipc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id4wipA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology240 — Ribosomal Protein L25; Chain P
Homologous superfamily homologous superfamily130
Domain ID domain_id4wipB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology240 — Ribosomal Protein L25; Chain P
Homologous superfamily homologous superfamily130
Domain ID domain_id4wipC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology240 — Ribosomal Protein L25; Chain P
Homologous superfamily homologous superfamily130

8. Citations (1)

9. Files and Curves (10)