› 1usd

X-ray diffraction
1.7Å resolution

human VASP tetramerisation domain L352M

Released:
DOI: 10.2210/pdb1usd/pdb
PDB entry 1usd coloured by chain, front view.
PDB entry 1usd coloured by chain, side view.
PDB entry 1usd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.
Kühnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV
Proc Natl Acad Sci U S A 101 17027-32 (2004)
PMID: 15569942

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156223 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vasodilator-stimulated phosphoprotein Chain: A
Molecule details ›
Chain: A
Length: 45 amino acids
Theoretical weight: 5.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50552 (Residues: 336-380; Coverage: 12%)
Gene name: VASP
Sequence domains: VASP tetramerisation domain
Structure domains: Vasodilator-stimulated phosphoprotein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I4
Unit cell:
a: 29.648Å b: 29.648Å c: 100.444Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.211 0.224
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Ena/VASP: towards resolving a pointed controversy at the barbed end.
Bear et al. (2009)
10 more

8 mentions without citation

The Structure and Topology of α-Helical Coiled Coils.
Lupas et al. (2017)
7 more