› 2jd5

X-ray diffraction
2.5Å resolution

Sky1p bound to Npl3p-derived substrate peptide

Released:
DOI: 10.2210/pdb2jd5/pdb
PDB entry 2jd5 coloured by chain, front view.
PDB entry 2jd5 coloured by chain, side view.
PDB entry 2jd5 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The RGG domain of Npl3p recruits Sky1p through docking interactions.
Lukasiewicz R, Nolen B, Adams JA, Ghosh G
J Mol Biol 367 249-61 (2007)
PMID: 17239901

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169593 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase SKY1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 43.01 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03656 (Residues: 138-742; Coverage: 50%)
Gene names: SKY1, YM8261.10C, YMR216C
Sequence domains: Protein kinase domain
Structure domains:
Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 Chain: C
Molecule details ›
Chain: C
Length: 7 amino acids
Theoretical weight: 904 Da
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: Q01560 (Residues: 408-414; Coverage: 2%)
Gene names: D9461.19, MTR13, MTS1, NAB1, NOP3, NPL3, YDR432W

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 72.328Å b: 88.558Å c: 134.408Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.255
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

1 review citation

Phosphorylation mechanism and structure of serine-arginine protein kinases.
Ghosh et al. (2011)
16 other articles

1 mention without citation

Mapping Causal Variants with Single-Nucleotide Resolution Reveals Biochemical Drivers of Phenotypic Change.
She et al. (2018)