Crystal structure of C-terminal modified tau peptide-hybrid 4.2E-I with 14-3-3SIGMA

Structure

x-ray diffraction · 3 distinct chains · 77% helix, 0% strand (DSSP).

Ligands and binding sites

• D3W · (2~{R})-2-[(~{R})-(2-methoxyphenyl)-phenyl-methyl]pyrrolidine · ligand · 2 copies · chains A, B, C, D
• ACE · Acetyl group · ligand · chains B
• NA · Sodium ion · metal · 7 copies · chains A, C
• CL · Chloride ion · ion · 2 copies · chains C

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

Pockets

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

Interfaces

3 interfaces between chains.

• A–B · 568 Ų buried · 12 hydrogen bonds · protein-protein
• C–D · 440 Ų buried · 11 hydrogen bonds · protein-protein
• A–C · 192 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent, 2 modified (covalent ligand, phosphorylation).

Compared structures

• 6FAU · Crystal structure of C-terminal modified Tau peptide-hybrid 4.2e-I with 14-3-3sigma · 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 C against A, TM-score 0.95

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 6FAU · PDBe 6FAU · UniProt P31947