X-ray diffraction
1.5Å resolution

Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation


Function and Biology Details

Sequence domain:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 359 amino acids
Theoretical weight: 40.09 KDa
Source organism: Oryctolagus cuniculus
  • Canonical: P68135 (Residues: 3-377; Coverage: 95%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
Protein spire Chain: S
Molecule details ›
Chain: S
Length: 38 amino acids
Theoretical weight: 4.31 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
  • Canonical: Q9U1K1 (Residues: 448-485; Coverage: 4%)
Gene names: CG10076, p150-Spir, spir

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 52.96Å b: 71.81Å c: 100.72Å
α: 90° β: 90° γ: 90°
R R work R free
0.174 0.172 0.216
Expression system: Escherichia coli