› 3bwj

X-ray diffraction
2.3Å resolution

Complex of PKA with the bisubstrate protein kinase inhibitor lead compound Arc-1034

Released:
DOI: 10.2210/pdb3bwj/pdb
PDB entry 3bwj coloured by chain, front view.
PDB entry 3bwj coloured by chain, side view.
PDB entry 3bwj coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural analysis of ARC-type inhibitor (ARC-1034) binding to protein kinase A catalytic subunit and rational design of bisubstrate analogue inhibitors of basophilic protein kinases.
Lavogina D, Lust M, Viil I, König N, Raidaru G, Rogozina J, Enkvist E, Uri A, Bossemeyer D
J Med Chem 52 308-21 (2009)
PMID: 19143565

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-dependent protein kinase catalytic subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 40.79 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00517 (Residues: 2-351; Coverage: 100%)
Gene name: PRKACA
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ARX 2 x ARX
2 modified residues:
Ligand SEP 2 x SEP
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 71.188Å b: 72.632Å c: 77.221Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.249
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Bisubstrate inhibitors of protein kinases: from principle to practical applications.
Lavogina et al. (2010)
1 more

2 mentions without citation

Protein kinase-inhibitor database: structural variability of and inhibitor interactions with the protein kinase P-loop.
Patel et al. (2010)
1 more