Ternary complex of 14-3-3 sigma, P27PT198 phosphopeptide, and WQ147

Structure

x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).

Ligands and binding sites

• 0I2 · (4~{S})-~{N}-[(5-carbamimidoyl-3-phenyl-thiophen-2-yl) methyl]oxepane-4-carboxamide · ligand · chains A
• MG · Magnesium ion · metal · 3 copies · chains A
• CL · Chloride ion · ion · chains A

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

Pockets

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

Interfaces

1 interface between chains.

• A–P · 449 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation, phosphorylation).

Compared structures

• 7ORS · Ternary complex of 14-3-3 sigma, p27pT198 phosphopeptide, and WQ147 · the same entry in another collection · chain A against A, TM-score 1.00
• P31947 · AlphaFold monomer V2.0 prediction for 14-3-3 protein sigma (P31947) · a predicted model of the same protein · chain A against A, TM-score 0.95
• P46527 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase inhibitor 1B (P46527) · a predicted model of the same protein · chain P against A, TM-score 0.71

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 P31947
• Every structure of UniProt P46527
• Elsewhere: RCSB PDB 7ORS · PDBe 7ORS · UniProt P31947 · UniProt P46527