TEAD4 (216-434);E263A+Y429F complexed with yap peptide (60- 100);S94A and myristoate (covalently bound to LYS344, not CYS367!) at 1.65A (P41212 crystal form); myristoylation was done by adding myr-CoA

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 44% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · chains L
• MYR · Myristic acid · ligand · chains A
• PO4 · Phosphate ion · ion · chains A

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

1 interface between chains.

• A–L · 1357 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 lipid (covalent ligand, myristoylation).

Compared structures

• 6GEI · TEAD4 (216-434);E263A+Y429F complexed with yap peptide (60- 100);S94A and myristoate… · the same entry in another collection · chain A against A, 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 0.95
• P46937 · AlphaFold monomer V2.0 prediction for transcriptional coactivator YAP1 (P46937) · a predicted model of the same protein · chain L against A, TM-score 0.43

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 P46937
• Elsewhere: RCSB PDB 6GEI · PDBe 6GEI · UniProt Q15561 · UniProt P46937