› 1use

X-ray diffraction
1.3Å resolution

human VASP tetramerisation domain

Released:
DOI: 10.2210/pdb1use/pdb
PDB entry 1use coloured by chain, front view.
PDB entry 1use coloured by chain, side view.
PDB entry 1use 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: 5.3 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: 29.701Å b: 29.701Å c: 100.192Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.196
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

17 mentions without citation

Macromolecular ab initio phasing enforcing secondary and tertiary structure.
Millán et al. (2015)
16 more