14-3-3SIGMA in complex with a TASK3 peptide stabilized by semi- synthetic natural product Fc-nac

Structure

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

Ligands and binding sites

• EZ5 · ~{N}-[(2~{S})-2-[(1~{E},3~{R},4~{S},8~{R},9~{R},10~{R}, 11~{S},14~{S})-14-(methoxymethyl)-3,10-dimethyl-8-[(2~{S},3~{R},4~{S},5~{S},6~{R})-6-(2-methylbut-3-en-2-yloxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,9-bis(oxidanyl)-6-tricyclo[9.3.0.0^{3,7}]tetradeca-1,6-dienyl]propyl]ethanamide · ligand · chains A, P
• NA · Sodium ion · metal · 2 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 · 493 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

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

Compared structures

• 6GHP · 14-3-3sigma in complex with a TASK3 peptide stabilized by semi-synthetic natural product… · 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
• Q9NPC2 · AlphaFold monomer V2.0 prediction for potassium channel subfamily K member 9 (Q9NPC2) · a predicted model of the same protein · chain P against A, TM-score 0.70

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 Q9NPC2
• Elsewhere: RCSB PDB 6GHP · PDBe 6GHP · UniProt P31947 · UniProt Q9NPC2