› 1q97

X-ray diffraction
2.3Å resolution

The structure of the Saccharomyces cerevisiae SR protein kinase, Sky1p, with bound ATP

Released:
DOI: 10.2210/pdb1q97/pdb
PDB entry 1q97 coloured by chain, front view.
PDB entry 1q97 coloured by chain, side view.
PDB entry 1q97 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Nucleotide-induced conformational changes in the Saccharomyces cerevisiae SR protein kinase, Sky1p, revealed by X-ray crystallography.
Nolen B, Ngo J, Chakrabarti S, Vu D, Adams JA, Ghosh G
Biochemistry 42 9575-85 (2003)
PMID: 12911299

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 43.03 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03656 (Residues: 138-742; Coverage: 50%)
Gene names: SKY1, YM8261.10C, YMR216C
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 2 x MG
Ligand SO4 2 x SO4
Ligand ATP 1 x ATP
Ligand NI 1 x NI
Ligand ADN 1 x ADN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 71.823Å b: 88.692Å c: 133.495Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.264
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

7 mentions without citation

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