› 1how

X-ray diffraction
2.1Å resolution

THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST

Released:
DOI: 10.2210/pdb1how/pdb
PDB entry 1how coloured by chain, front view.
PDB entry 1how coloured by chain, side view.
PDB entry 1how coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The structure of Sky1p reveals a novel mechanism for constitutive activity.
Nolen B, Yun CY, Wong CF, McCammon JA, Fu XD, Ghosh G
Nat Struct Biol 8 176-83 (2001)
PMID: 11175909

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase SKY1 Chain: A
Molecule details ›
Chain: A
Length: 373 amino acids
Theoretical weight: 43.01 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03656 (Residues: 138-304, 539-742; Coverage: 50%)
Gene names: SKY1, YM8261.10C, YMR216C
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 6 x SO4
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 73.403Å b: 88.322Å c: 135.952Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.255
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Regulation of protein kinases; controlling activity through activation segment conformation.
Nolen et al. (2004)
11 more

3 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
2 more