7wn3

Cryo-EM structure of VWF D'D3 dimer (2M mutant) complexed with D1D2 at 3.29 angstron resolution (2 units)

Method: ELECTRON MICROSCOPY Dmax: 218.8 Å Quality: GOOD

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

von Willebrand antigen 2

Homo sapiens

UniProt P04275

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 23–763 Chain B; UniProt 23–763 Chain C; UniProt 764–1241 Chain D; UniProt 764–1241 Chain E; UniProt 23–763 Chain F; UniProt 764–1241 Chain G; UniProt 23–763 Chain H; UniProt 764–1241 Fragment:D1D2 domain Fragment:;D'D3 domain ; Mutation:R1136M,E1143M CA CALCIUM ION × 16 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 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.

46 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VWF_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–741; UniProt 23–763 Author chain B; PDBConstruct 1–741; UniProt 23–763 Author chain E; PDBConstruct 1–741; UniProt 23–763 Author chain G; PDBConstruct 1–741; UniProt 23–763 Author chain C; PDBConstruct 1–478; UniProt 764–1241 Author chain D; PDBConstruct 1–478; UniProt 764–1241 Author chain F; PDBConstruct 1–478; UniProt 764–1241 Author chain H; PDBConstruct 1–478; UniProt 764–1241

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 7wn3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7wn3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7wn3
Deposition date deposition_date2022-01-17
Structure title titleCryo-EM structure of VWF D'D3 dimer (2M mutant) complexed with D1D2 at 3.29 angstron resolution (2 units)
Keywords keywords;blood, VWF, von Willebrand factor, von Willebrand disease, blood coagulation, blood clotting, multimer assembly, VWF assembly, D'D3 domain, D1D2 domain, D'D3 dimer, D1D2 Dimer, VWF Tube, repeating unit ;; BLOOD CLOTTING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier75.49
Radius of gyration Rg (electron density) rg_electron75.74
Forward intensity I(0) i04448580000.00
Molecular weight molecular_weight526790.0 kDa
Excluded volume excluded_volume642400 ų
Envelope volume envelope_volume1129300 ų
Hydration-shell volume shell_volume124440 ų
Envelope diameter envelope_diameter249.1
Shell Rg shell_rg73.17
Envelope Rg envelope_rg73.50
Shape Rg shape_rg75.70
Total Rg total_rg75.82
Total atoms total_atoms36560
Residues n_residues4756
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 dmax218.8
Rg (real space) rg_real75.66
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real4.4450e+09
I(0) uncertainty (real space) i0_real_error8.6650e+07
Rg (reciprocal space) rg_reciprocal74.04
I(0) (reciprocal space) i0_reciprocal4432000000.0000
Solution quality estimate total_estimate0.8202
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.5
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.872
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0047
Highest regularization parameter α highest_alpha254500000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)