2otx

X-ray diffraction
2.6Å resolution

Crystal Structure of A N-terminal Fragment of SKAP-HOM Containing both the Helical Dimerization Domain and the PH Domain

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Src kinase-associated phosphoprotein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 24.17 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q3UND0 (Residues: 12-222; Coverage: 59%)
Gene names: Prap, Ra70, Saps, Scap2, Skap2, Skap55r
Sequence domains: PH domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: C2
Unit cell:
a: 106.205Å b: 56.742Å c: 89.115Å
α: 90° β: 95.82° γ: 90°
R-values:
R R work R free
0.181 0.179 0.216
Expression system: Escherichia coli BL21(DE3)