Crystal structure of human 14-3-3 sigma in complex with task-3 peptide and stabilizer 16-O-me-Fc-H

Structure

x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).

Ligands and binding sites

• 0V4 · (4R,5R,6R,6aS,9S,9aE,10aR)-5-hydroxy-9-(methoxymethyl)-6,10a-dimethyl-3-(propan-2-yl)-1,2,4,5,6,6a,7,8,9,10a-decahydrodicyclopenta[a,d][8]annulen-4-yl alpha-D-glucopyranoside · ligand · chains A, P
• MG · Magnesium ion · metal · 2 copies · 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, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–P · 532 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

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

Compared structures

• 4FR3 · Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilizer… · 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 0.96

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
• Elsewhere: RCSB PDB 4FR3 · PDBe 4FR3 · UniProt P31947