X-ray structure of TEAD4 (wildtype) complexed with yap (wildtype): the role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface

Structure

x-ray diffraction · 2 distinct chains.

Ligands and binding sites

• MYR · Myristic acid · ligand · chains A
• GOL · Glycerol · additive · chains A, L

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

Compared structures

• 6GE3 · X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual… · 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 0.98
• P46937 · AlphaFold monomer V2.0 prediction for transcriptional coactivator YAP1 (P46937) · a predicted model of the same protein · chain L against A, TM-score 0.44

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 6GE3 · PDBe 6GE3 · UniProt Q15561 · UniProt P46937