Crystal structure of mertk in complex with a type 1.5 aminopyridine inhibitor

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Ligands and binding sites

• R6K · 2-azanyl-~{N}-[(1~{S},2~{S})-2-[[4-[4-[(4-methylpiperazin-1-yl) methyl]phenyl]phenyl]methoxy]cyclopentyl]-5-(1-methylpyrazol-4-yl)pyridine-3-carboxamide · ligand · chains A
• CL · Chloride ion · ion · 6 copies · chains A
• EDO · 1,2-ethanediol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Compared structures

• 7AAZ · Crystal structure of MerTK in complex with a type 1.5 aminopyridine inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
• Q12866 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase mer (Q12866) · a predicted model of the same protein · chain A against A, TM-score 0.90

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q12866
• Elsewhere: RCSB PDB 7AAZ · PDBe 7AAZ · UniProt Q12866