› 4ra5

X-ray diffraction
2.61Å resolution

Human Protein Kinase C THETA IN COMPLEX WITH LIGAND COMPOUND 11a (6-[(1,3-Dimethyl-azetidin-3-yl)-methyl-amino]-4(R)-methyl-7-phenyl-2,10-dihydro-9-oxa-1,2,4a-triaza-phenanthren-3-one)

Released:
DOI: 10.2210/pdb4ra5/pdb
PDB entry 4ra5 coloured by chain, front view.
PDB entry 4ra5 coloured by chain, side view.
PDB entry 4ra5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Optimized protein kinase Cθ (PKCθ) inhibitors reveal only modest anti-inflammatory efficacy in a rodent model of arthritis.
George DM, Breinlinger EC, Argiriadi MA, Zhang Y, Wang J, Bansal-Pakala P, Duignan DB, Honore P, Lang Q, Mittelstadt S, Rundell L, Schwartz A, Sun J, Edmunds JJ
J Med Chem 58 333-46 (2015)
PMID: 25254961

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein kinase C theta type Chains: A, B
Molecule details ›
Chains: A, B
Length: 334 amino acids
Theoretical weight: 39.6 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04759 (Residues: 374-706; Coverage: 47%)
Gene names: PRKCQ, PRKCT
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 3L0 2 x 3L0
Ligand NA 1 x NA
Ligand EDO 2 x EDO
1 modified residue:
Ligand SEP 4 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 74.822Å b: 77.026Å c: 147.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.277
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Dynamics and Membrane Interactions of Protein Kinase C.
Igumenova TI. (2015)
10 other articles

2 mentions without citation

Kinase Atlas: Druggability Analysis of Potential Allosteric Sites in Kinases.
Yueh et al. (2019)
1 more