Structure of human JNK1 in complex with SCH772984 and the amppnp- hydrolysed triphosphate revealing the second type-I binding mode

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

Ligands and binding sites

• 38Z · (3R)-1-(2-oxo-2-{4-[4-(pyrimidin-2-yl)phenyl]piperazin-1-yl}ethyl)-N-[3-(pyridin-4-yl)-2H-indazol-5-yl]pyrrolidine-3-carboxamide · ligand · chains A
• ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
• MG · Magnesium ion · metal · chains A
• EDO · 1,2-ethanediol · additive · 22 copies · chains A
• EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

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

Compared structures

• 4QTD · Structure of human JNK1 in complex with SCH772984 and the AMPPNP-hydrolysed triphosphate… · the same entry in another collection · chain A against A, TM-score 1.00
• P45983 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 8 (P45983) · a predicted model of the same protein · chain A 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 P45983
• Elsewhere: RCSB PDB 4QTD · PDBe 4QTD · UniProt P45983