Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase mer in complex with inhibitor UNC3437

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).

Ligands and binding sites

• 9VS · cis-4-[(2-[(4-{[4-(1,3-dioxolan-2-yl)pyridin-2-yl]ethynyl}phenyl)amino]-5-{4-[(4-methylpiperazin-1-yl)methyl]phenyl}pyrimidin-4-yl)amino]cyclohexan-1-ol · ligand · 2 copies · chains A, B
• MG · Magnesium ion · metal · chains B
• CL · Chloride ion · ion · 5 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1058 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

• 6MEP · Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase… · 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 B against A, TM-score 0.98

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 6MEP · PDBe 6MEP · UniProt Q12866