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

Structure

x-ray diffraction · 5 distinct chains · 83% helix, 0% strand (DSSP).

Ligands and binding sites

• ETE · 2-{2-[2-2-(methoxy-ethoxy)-ethoxy]-ethoxy}-ethanol · ligand · 2 copies · chains A, B, C, D

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

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

11 interfaces between chains.

• A–B · 1170 Ų buried · 11 hydrogen bonds · protein-protein
• C–D · 1031 Ų buried · 11 hydrogen bonds · protein-protein
• D–F · 866 Ų buried · 17 hydrogen bonds · protein-protein
• B–E · 855 Ų buried · 18 hydrogen bonds · protein-protein
• B–C · 395 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

• 6HEP · Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768 · the same entry in another collection · chain F against F, TM-score 1.00
• P31946 · AlphaFold monomer V2.0 prediction for 14-3-3 protein BETA/ALPHA (P31946) · a predicted model of the same protein · chain C 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 E against A, TM-score 0.29

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 P31946
• Every structure of UniProt P13569
• Elsewhere: RCSB PDB 6HEP · PDBe 6HEP · UniProt P31946 · UniProt P13569