8dvm

Crystal structure of LRP6 E3E4 in complex with disulfide constrained peptide E3.6

Method: X-RAY DIFFRACTION Dmax: 103.0 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 × 2 其他Polymer 4 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 631–1253 Non-standard monomer:Yes (specific site not provided by mmCIF) E3.6 Disulfide constrained peptide × 1 ;alpha-L-fucopyranose-(1-3)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 3 EDO 1,2-ETHANEDIOL × 14 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.3;293 K;100 mM MES pH 6.3, 12% PEG 20K Resolution 2.00 Å R-free 0.221

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 2–624; UniProt 631–1253

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 8dvm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dvm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dvm
Deposition date deposition_date2022-07-29
Structure title titleCrystal structure of LRP6 E3E4 in complex with disulfide constrained peptide E3.6
Keywords keywordsLRP6, E3E4, Wnt Signaling, SIGNALING PROTEIN, Disulfide constrained peptide, Wnt agonism; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.19
Radius of gyration Rg (electron density) rg_electron29.52
Forward intensity I(0) i094452100.00
Molecular weight molecular_weight75223.0 kDa
Excluded volume excluded_volume93503 ų
Envelope volume envelope_volume113920 ų
Hydration-shell volume shell_volume32684 ų
Envelope diameter envelope_diameter108.4
Shell Rg shell_rg35.89
Envelope Rg envelope_rg29.74
Shape Rg shape_rg29.50
Total Rg total_rg30.15
Total atoms total_atoms5275
Residues n_residues626
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 dmax103.0
Rg (real space) rg_real30.32
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real9.4450e+07
I(0) uncertainty (real space) i0_real_error1.4900e+06
Rg (reciprocal space) rg_reciprocal30.27
I(0) (reciprocal space) i0_reciprocal94450000.0000
Solution quality estimate total_estimate0.8563
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.432
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28760000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.762; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.876; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)