› 5ceo

X-ray diffraction
2.28Å resolution

DLK in complex with inhibitor 2-((6-(3,3-difluoropyrrolidin-1-yl)-4-(1-(oxetan-3-yl)piperidin-4-yl)pyridin-2-yl)amino)isonicotinonitrile

Released:
DOI: 10.2210/pdb5ceo/pdb
PDB entry 5ceo coloured by chain, front view.
PDB entry 5ceo coloured by chain, side view.
PDB entry 5ceo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Scaffold-Hopping and Structure-Based Discovery of Potent, Selective, And Brain Penetrant N-(1H-Pyrazol-3-yl)pyridin-2-amine Inhibitors of Dual Leucine Zipper Kinase (DLK, MAP3K12).
Patel S, Harris SF, Gibbons P, Deshmukh G, Gustafson A, Kellar T, Lin H, Liu X, Liu Y, Liu Y, Ma C, Scearce-Levie K, Ghosh AS, Shin YG, Solanoy H, Wang J, Wang B, Yin J, Siu M, Lewcock JW
J Med Chem 58 8182-99 (2015)
PMID: 26431428

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-171415 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase kinase kinase 12 Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 34.02 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q12852 (Residues: 115-402; Coverage: 34%)
Gene names: MAP3K12, ZPK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 50D 1 x 50D
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 57.82Å b: 39.04Å c: 62.79Å
α: 90° β: 107.37° γ: 90°
R-values:
R R work R free
0.19 0.187 0.248
Expression system: Trichoplusia ni

Quick links

Citations

8 review citations

Kinase inhibitors: the road ahead.
Ferguson et al. (2018)
7 more

2 mentions without citation

Molden 2.0: quantum chemistry meets proteins.
Schaftenaar et al. (2017)
1 more