14-3-3C in complex with CPP7

Structure

x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).

Ligands and binding sites

• PGE · Triethylene glycol · additive · 2 copies · chains A
• PEG · Di(hydroxyethyl)ether · additive · chains A
• GOL · Glycerol · additive · chains A
• ACT · Acetate ion · additive · chains A, P

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 · 611 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

• 5NWJ · 14-3-3c in complex with CPP7 · the same entry in another collection · chain A against A, TM-score 1.00
• P93343 · AlphaFold monomer V2.0 prediction for 14-3-3-like protein C (P93343) · a predicted model of the same protein · chain A against A, TM-score 0.98
• Q39128 · AlphaFold monomer V2.0 prediction for potassium channel KAT1 (Q39128) · a predicted model of the same protein · chain P against A, TM-score 0.56

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 P93343
• Every structure of UniProt Q39128
• Elsewhere: RCSB PDB 5NWJ · PDBe 5NWJ · UniProt P93343 · UniProt Q39128