7wpr

VWF D'D3 dimer complexed with D1D2 at 4.39 angstron resolution(VWF tube)

Method: ELECTRON MICROSCOPY Dmax: 302.8 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 × 32 PDB declaration: 32-meric(32) 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 23–763 Chain G; UniProt 23–763 Chain H; UniProt 23–763 Chain I; UniProt 23–763 Chain J; UniProt 23–763 Chain K; UniProt 23–763 Chain L; UniProt 23–763 Chain M; UniProt 23–763 Chain N; UniProt 23–763 Chain O; UniProt 23–763 Chain P; UniProt 23–763 Chain Q; UniProt 23–763 Chain R; UniProt 23–763 Chain S; UniProt 764–1241 Chain T; UniProt 764–1241 Chain U; UniProt 764–1241 Chain V; UniProt 764–1241 Chain W; UniProt 764–1241 Chain X; UniProt 764–1241 Chain Y; UniProt 764–1241 Chain Z; UniProt 764–1241 Chain a; UniProt 764–1241 Chain b; UniProt 764–1241 Chain c; UniProt 764–1241 Chain d; UniProt 764–1241 Chain e; UniProt 764–1241 Chain f; UniProt 764–1241 Fragment:D1D2 domain Fragment:;D'D3 domain ; NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 42 CA CALCIUM ION × 56 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.39 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 F; PDBConstruct 1–741; UniProt 23–763 Author chain G; PDBConstruct 1–741; UniProt 23–763 Author chain H; PDBConstruct 1–741; UniProt 23–763 Author chain I; PDBConstruct 1–741; UniProt 23–763 Author chain J; PDBConstruct 1–741; UniProt 23–763 Author chain K; PDBConstruct 1–741; UniProt 23–763 Author chain L; PDBConstruct 1–741; UniProt 23–763 Author chain M; PDBConstruct 1–741; UniProt 23–763 Author chain N; PDBConstruct 1–741; UniProt 23–763 Author chain O; PDBConstruct 1–741; UniProt 23–763 Author chain P; PDBConstruct 1–741; UniProt 23–763 Author chain Q; PDBConstruct 1–741; UniProt 23–763 Author chain R; 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 S; PDBConstruct 1–478; UniProt 764–1241 Author chain T; PDBConstruct 1–478; UniProt 764–1241 Author chain U; PDBConstruct 1–478; UniProt 764–1241 Author chain V; PDBConstruct 1–478; UniProt 764–1241 Author chain W; PDBConstruct 1–478; UniProt 764–1241 Author chain X; PDBConstruct 1–478; UniProt 764–1241 Author chain Y; PDBConstruct 1–478; UniProt 764–1241 Author chain Z; PDBConstruct 1–478; UniProt 764–1241 Author chain a; PDBConstruct 1–478; UniProt 764–1241 Author chain b; PDBConstruct 1–478; UniProt 764–1241 Author chain c; PDBConstruct 1–478; UniProt 764–1241 Author chain d; PDBConstruct 1–478; UniProt 764–1241 Author chain e; PDBConstruct 1–478; UniProt 764–1241 Author chain f; 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 7wpr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7wpr
Deposition date deposition_date2022-01-24
Structure title titleVWF D'D3 dimer complexed with D1D2 at 4.39 angstron resolution(VWF tube)
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_guinier
Radius of gyration Rg (electron density) rg_electron118.50
Forward intensity I(0) i069239200000.00
Molecular weight molecular_weight2098000.0 kDa
Excluded volume excluded_volume2558100 ų
Envelope volume envelope_volume5821200 ų
Hydration-shell volume shell_volume409330 ų
Envelope diameter envelope_diameter396.3
Shell Rg shell_rg125.40
Envelope Rg envelope_rg107.50
Shape Rg shape_rg118.50
Total Rg total_rg118.60
Total atoms total_atoms145668
Residues n_residues19024
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 dmax302.8
Rg (real space) rg_real116.00
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real6.6380e+10
I(0) uncertainty (real space) i0_real_error1.3420e+09
Rg (reciprocal space) rg_reciprocal126.20
I(0) (reciprocal space) i0_reciprocal71050000000.0000
Solution quality estimate total_estimate0.8867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary163.1
Skewness Skewness skewness-0.166
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha1.3290
Highest regularization parameter α highest_alpha2078000000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 0.959; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; 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)