6jck

Complex structure of Axin-DIX and Dvl2-DIX

Method: X-RAY DIFFRACTION Dmax: 58.1 Å Quality: GOOD

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

Axin-1

Homo sapiens

UniProt O15169

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 745–826 Mutation:Y760D Segment polarity protein dishevelled homolog DVL-2 × 1 (O14641) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;25% (w/v) PEG1500, 0.1 M Malonate-Imidazole-Borate buffer pH 7.0 Resolution 3.09 Å R-free 0.290

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.

15 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AXIN1_HUMAN
Isoform O15169-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–82; UniProt 745–826

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 12–93 Mutation:V67A,K68A Axin-1 × 1 (O15169) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;25% (w/v) PEG1500, 0.1 M Malonate-Imidazole-Borate buffer pH 7.0 Resolution 3.09 Å R-free 0.290

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–82; UniProt 12–93

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 6jck

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6jck
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6jck
Deposition date deposition_date2019-01-29
Structure title titleComplex structure of Axin-DIX and Dvl2-DIX
Keywords keywordsWnt signalling, 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_guinier17.34
Radius of gyration Rg (electron density) rg_electron15.99
Forward intensity I(0) i04857760.00
Molecular weight molecular_weight16649.0 kDa
Excluded volume excluded_volume21268 ų
Envelope volume envelope_volume25347 ų
Hydration-shell volume shell_volume13722 ų
Envelope diameter envelope_diameter57.6
Shell Rg shell_rg21.39
Envelope Rg envelope_rg16.26
Shape Rg shape_rg15.94
Total Rg total_rg17.22
Total atoms total_atoms1179
Residues n_residues145
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 dmax58.1
Rg (real space) rg_real17.30
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real4.8580e+06
I(0) uncertainty (real space) i0_real_error6.0230e+04
Rg (reciprocal space) rg_reciprocal17.30
I(0) (reciprocal space) i0_reciprocal4858000.0000
Solution quality estimate total_estimate0.8749
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.308
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha1519000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6jcka_
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.15.1.8 — DIX domain
Domain ID domain_idd6jckb_
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 (2 domains)

Domain ID domain_id6jckA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology240 — Ribosomal Protein L25; Chain P
Homologous superfamily homologous superfamily130
Domain ID domain_id6jckB00
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)