Crystal structure of ERK1 covalently bound to SM1-71

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Ligands and binding sites

• 6H3 · N-{2-[(5-chloro-2-{[4-(4-methylpiperazin-1-yl) phenyl]amino}pyrimidin-4-yl)amino]phenyl}propanamide · ligand · 2 copies · chains A, B
• EWH · ~{N}-[2-[[5-chloranyl-2-[[4-(4-methylpiperazin-1-yl) phenyl]amino]pyrimidin-4-yl]amino]phenyl]prop-2-enamide · ligand · chains A
• SO4 · Sulfate ion · ion · 2 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 5 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1092 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 6GES · Crystal structure of ERK1 covalently bound to SM1-71 · the same entry in another collection · chain A against A, TM-score 1.00
• P27361 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 3 (P27361) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P27361
• Elsewhere: RCSB PDB 6GES · PDBe 6GES · UniProt P27361