5d9h

X-ray diffraction
3.1Å resolution

Crystal structure of SPAK (STK39) dimer in the basal activity state

Released:
Source organism: Mus musculus
Primary publication:
Domain-Swapping Switch Point in Ste20 Protein Kinase SPAK.
Biochemistry 54 5063-71 (2015)
PMID: 26208601

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-195541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
STE20/SPS1-related proline-alanine-rich protein kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 348 amino acids
Theoretical weight: 39.18 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Z1W9 (Residues: 63-403; Coverage: 61%)
Gene names: Spak, Stk39
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 72.386Å b: 56.105Å c: 99.958Å
α: 90° β: 108.28° γ: 90°
R-values:
R R work R free
0.24 0.236 0.269
Expression system: Escherichia coli