7o86

X-ray diffraction
1.73Å resolution

1.73A X-ray crystal structure of the conserved C-terminal (CCT) of human SPAK

Released:
Source organism: Homo sapiens

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-193704 (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: 106 amino acids
Theoretical weight: 11.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UEW8 (Residues: 441-545; Coverage: 19%)
Gene names: PASK, SPAK, STK39
Sequence domains: Oxidative-stress-responsive kinase 1 C-terminal domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 39.611Å b: 50.549Å c: 103.798Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.24
Expression system: Escherichia coli