› 3a8w

X-ray diffraction
2.1Å resolution

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-154422 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein kinase C iota type Chains: A, B
Molecule details ›
Chains: A, B
Length: 345 amino acids
Theoretical weight: 39.85 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P41743 (Residues: 249-588; Coverage: 57%)
Gene names: DXS1179E, PRKCI
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 2 x ATP
Ligand SO4 1 x SO4
1 modified residue:
Ligand TPO 4 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 85.039Å b: 89.136Å c: 206.395Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.247 0.301
Expression system: Spodoptera frugiperda

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Citations

3 review citations

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

14 mentions without citation

Autoregulation of kinase dephosphorylation by ATP binding in AGC protein kinases.
Chan et al. (2012)
13 more