3s2k

Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.

Method: X-RAY DIFFRACTION Dmax: 159.3 Å Quality: GOOD

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

Low-density lipoprotein receptor-related protein 6

Homo sapiens

UniProt O75581

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 4 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 630–1246 Chain B; UniProt 630–1246 Fragment:ectodomain repeats 3, 4 UNP residues 630-1246 Dickkopf-related protein 1 × 1 (O94907) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;10-15% PEG3350, 100 mM Tris-Cl (pH 8.5), 100 mM Lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.80 Å R-free 0.251

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.

27 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LRP6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–619; UniProt 630–1246 Author chain B; PDBConstruct 3–619; UniProt 630–1246

Dickkopf-related protein 1

Homo sapiens

UniProt O94907

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 4 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 178–266 Fragment:C-terminal domain, UNP residues 178-266 Low-density lipoprotein receptor-related protein 6 × 2 (O75581) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;295 K;10-15% PEG3350, 100 mM Tris-Cl (pH 8.5), 100 mM Lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.80 Å R-free 0.251

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DKK1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 4–92; UniProt 178–266

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 3s2k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3s2k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3s2k
Deposition date deposition_date2011-05-16
Structure title titleStructural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.
Keywords keywordswnt co-receptor, beta-propeller, EGF domain, wnt signaling, wnt inhibitor, glycosylation, 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_guinier41.87
Radius of gyration Rg (electron density) rg_electron41.92
Forward intensity I(0) i0359078000.00
Molecular weight molecular_weight150280.0 kDa
Excluded volume excluded_volume186380 ų
Envelope volume envelope_volume249590 ų
Hydration-shell volume shell_volume52901 ų
Envelope diameter envelope_diameter171.2
Shell Rg shell_rg43.58
Envelope Rg envelope_rg41.72
Shape Rg shape_rg41.87
Total Rg total_rg42.16
Total atoms total_atoms10557
Residues n_residues1298
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 dmax159.3
Rg (real space) rg_real42.19
Rg uncertainty (real space) rg_real_error2.47
I(0) (real space) i0_real3.5910e+08
I(0) uncertainty (real space) i0_real_error6.9790e+06
Rg (reciprocal space) rg_reciprocal41.87
I(0) (reciprocal space) i0_reciprocal359000000.0000
Solution quality estimate total_estimate0.8086
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.7
Skewness Skewness skewness0.574
Kurtosis Kurtosis kurtosis-0.031
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha108300000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.592; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.793; Smooth: 0.938

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id3s2kA01
Class class2 — Mainly Beta
Architecture architecture120 — 6 Propeller
Topology topology10 — Neuraminidase
Homologous superfamily homologous superfamily30 — TolB, C-terminal domain
Domain ID domain_id3s2kA02
Class class2 — Mainly Beta
Architecture architecture120 — 6 Propeller
Topology topology10 — Neuraminidase
Homologous superfamily homologous superfamily30 — TolB, C-terminal domain
Domain ID domain_id3s2kB01
Class class2 — Mainly Beta
Architecture architecture120 — 6 Propeller
Topology topology10 — Neuraminidase
Homologous superfamily homologous superfamily30 — TolB, C-terminal domain
Domain ID domain_id3s2kB02
Class class2 — Mainly Beta
Architecture architecture120 — 6 Propeller
Topology topology10 — Neuraminidase
Homologous superfamily homologous superfamily30 — TolB, C-terminal domain
Domain ID domain_id3s2kC00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology80 — Lipase, subunit A
Homologous superfamily homologous superfamily10 — Lipase, subunit A

8. Citations (1)

9. Files and Curves (10)