TEAD4 bound to a FAM181A peptide

Structure

x-ray diffraction · 3 distinct chains · 18% helix, 50% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 2 copies · chains A, L, B, M
• SO4 · Sulfate ion · ion · 5 copies · chains A, B, L
• NH2 · Amino group · ion · 2 copies · chains L, B, M

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 · 1096 Ų buried · 23 hydrogen bonds · protein-protein
• A–L · 738 Ų buried · 15 hydrogen bonds · protein-protein
• B–M · 727 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

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

Compared structures

• 6SEN · TEAD4 bound to a FAM181A peptide · the same entry in another collection · chain M against M, TM-score 1.00
• Q15561 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-3 (Q15561) · a predicted model of the same protein · chain A against A, TM-score 0.98
• Q8N9Y4 · AlphaFold monomer V2.0 prediction for protein FAM181A (Q8N9Y4) · a predicted model of the same protein · chain M against A, TM-score 0.59

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 Q15561
• Every structure of UniProt Q8N9Y4
• Elsewhere: RCSB PDB 6SEN · PDBe 6SEN · UniProt Q15561 · UniProt Q8N9Y4