Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase mer in complex with inhibitor UNC2434

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

Ligands and binding sites

• 6Q1 · 15-{4-[(4-methylpiperazin-1-yl)methyl]phenyl}-4,5,6,7,9,10,11,12-octahydro-2,16-(azenometheno)pyrrolo[2,1-d][1,3,5,9]te traazacyclotetradecin-8(3H)-one · ligand · 2 copies · chains A, B
• MG · Magnesium ion · metal · chains B
• CL · Chloride ion · ion · 6 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 · 1039 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

• 5K0K · 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 0.97

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 5K0K · PDBe 5K0K · UniProt Q12866