› 2z7s

X-ray diffraction
2.1Å resolution

Crystal Structure of the N-terminal Kinase Domain of Human RSK1 bound to Purvalnol A

Released:
DOI: 10.2210/pdb2z7s/pdb
PDB entry 2z7s coloured by chain, front view.
PDB entry 2z7s coloured by chain, side view.
PDB entry 2z7s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the N-terminal kinase domain of human RSK1 bound to three different ligands: Implications for the design of RSK1 specific inhibitors.
Ikuta M, Kornienko M, Byrne N, Reid JC, Mizuarai S, Kotani H, Munshi SK
Protein Sci 16 2626-35 (2007)
PMID: 17965187

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172282 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal protein S6 kinase alpha-1 Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 36.78 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q15418 (Residues: 33-353; Coverage: 44%)
Gene names: MAPKAPK1A, RPS6KA1, RSK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand P01 1 x P01
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 51.641Å b: 52.996Å c: 119.304Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.279 0.253 not available
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

AGC protein kinases: from structural mechanism of regulation to allosteric drug development for the treatment of human diseases.
Arencibia et al. (2013)
3 more

5 mentions without citation

Luteolin is a novel p90 ribosomal S6 kinase (RSK) inhibitor that suppresses Notch4 signaling by blocking the activation of Y-box binding protein-1 (YB-1).
Reipas et al. (2013)
4 more