Crystal structure of MST2 in complex with xmu-mp-1

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

Ligands and binding sites

• 5BS · 4-[(5,10-dimethyl-6-oxo-6,10-dihydro-5H-pyrimido[5,4-b]thieno[3,2-e][1,4]diazepin-2-yl)amino]benzenesulfonamide · ligand · 2 copies · chains A, B
• TPO · Phosphothreonine · ligand · 2 copies · chains B
• NA · Sodium ion · metal · 2 copies · chains A

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 483 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 covalent, 2 modified (covalent ligand, phosphorylation).

Compared structures

• 8A66 · Crystal structure of MST2 in complex with XMU-MP-1 · the same entry in another collection · chain A against A, TM-score 1.00
• Q13188 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase 3 (Q13188) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q13188
• Elsewhere: RCSB PDB 8A66 · PDBe 8A66 · UniProt Q13188