Crystal structure of human 14-3-3 zeta in complex with cftr R-domain peptide PS753-PS768

Structure

x-ray diffraction · 3 distinct chains · 79% helix, 0% strand (DSSP).

Ligands and binding sites

• GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A, B
• FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, B
• CL · Chloride ion · ion · 4 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–B · 921 Ų buried · 13 hydrogen bonds · protein-protein
• A–C · 909 Ų buried · 19 hydrogen bonds · protein-protein
• B–C · 605 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

• 5D2D · Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768 · the same entry in another collection · chain A against A, TM-score 1.00
• P63104 · AlphaFold monomer V2.0 prediction for 14-3-3 protein ZETA/DELTA (P63104) · a predicted model of the same protein · chain A against A, TM-score 0.98
• P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain C against A, TM-score 0.24

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 P63104
• Every structure of UniProt P13569
• Elsewhere: RCSB PDB 5D2D · PDBe 5D2D · UniProt P63104 · UniProt P13569