› 7a6o

X-ray diffraction
2.12Å resolution

Crystal Structure of the Complex of the Recombinant Von Willebrand Factor AIM-A1 domain and VHH81 at 2.1 Angstrom resolution

Released:
DOI: 10.2210/pdb7a6o/pdb
PDB entry 7a6o coloured by chain, front view.
PDB entry 7a6o coloured by chain, side view.
PDB entry 7a6o coloured by chain, top view.
Source organisms:
Primary publication:
Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module.
Arce NA, Cao W, Brown AK, Legan ER, Wilson MS, Xu ER, Berndt MC, Emsley J, Zhang XF, Li R
OpenAccess logo Nat Commun 12 2360 (2021)
PMID: 33883551

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-207984 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
von Willebrand factor Chain: A
Molecule details ›
Chain: A
Length: 205 amino acids
Theoretical weight: 23.45 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: L8E853 (Residues: 1262-1466; Coverage: 8%)
Gene name: VWF
Sequence domains: von Willebrand factor type A domain
VHH81 Nanobody fragment Chain: B
Molecule details ›
Chain: B
Length: 128 amino acids
Theoretical weight: 13.86 KDa
Source organism: Lama glama
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P43212
Unit cell:
a: 65.234Å b: 65.234Å c: 233.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.256
Expression systems:
  • Homo sapiens
  • Escherichia coli

Quick links

Citations

6 review citations

Contribution of the von Willebrand factor/ADAMTS13 imbalance to COVID-19 coagulopathy.
Seth et al. (2022)
5 more

3 mentions without citation

Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module.
Arce et al. (2021)
2 more