5gje

Three-dimensional reconstruction of human LRP6 ectodomain complexed with Dkk1

Method: ELECTRON MICROSCOPY Dmax: 137.4 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 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 20–630 Chain B; UniProt 631–1246 Fragment:UNP residues 20-630 Fragment:UNP residues 631-1246 Mutation:V1062I Dickkopf-related protein 1 × 1 (O94907) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PO4 PHOSPHATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 Resolution 21.00 Å

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–611; UniProt 20–630 Author chain B; PDBConstruct 1–616; UniProt 631–1246

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 5 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 182–266 Not recorded Low-density lipoprotein receptor-related protein 6 × 1 (O75581) Low-density lipoprotein receptor-related protein 6 × 1 (O75581) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PO4 PHOSPHATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 Resolution 21.00 Å

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–85; UniProt 182–266

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 5gje

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5gje
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5gje
Deposition date deposition_date2016-06-29
Structure title titleThree-dimensional reconstruction of human LRP6 ectodomain complexed with Dkk1
Keywords keywordsWnt signaling, Wnt co-receptor, LRP6, glycoprotein, antagonist, Dkk1, conformational change, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.65
Radius of gyration Rg (electron density) rg_electron43.22
Forward intensity I(0) i0343312000.00
Molecular weight molecular_weight149310.0 kDa
Excluded volume excluded_volume185480 ų
Envelope volume envelope_volume258690 ų
Hydration-shell volume shell_volume49347 ų
Envelope diameter envelope_diameter139.5
Shell Rg shell_rg49.51
Envelope Rg envelope_rg41.62
Shape Rg shape_rg43.19
Total Rg total_rg43.60
Total atoms total_atoms10493
Residues n_residues1293
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 dmax137.4
Rg (real space) rg_real43.59
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real3.4330e+08
I(0) uncertainty (real space) i0_real_error6.8780e+06
Rg (reciprocal space) rg_reciprocal43.65
I(0) (reciprocal space) i0_reciprocal343300000.0000
Solution quality estimate total_estimate0.8861
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary64.9
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.852
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha59380000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)