› 2ylf

X-ray diffraction
2.05Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170713 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein spire homolog 1 Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 25.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q08AE8 (Residues: 36-236; Coverage: 27%)
Gene names: KIAA1135, SPIR1, SPIRE1
Sequence domains: Kinase non-catalytic C-lobe domain
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 65.914Å b: 65.914Å c: 78.803Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.2 0.263
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Formins at a glance.
Breitsprecher et al. (2013)
7 more

3 mentions without citation

Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)•formin-2 formin SPIR interaction motif (FSI) complex.
Zeth et al. (2011)
2 more