X-ray diffraction
1.85Å resolution

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


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcriptional enhancer factor TEF-3 Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 25.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: Q15561 (Residues: 216-434; Coverage: 51%)
Gene names: RTEF1, TCF13L1, TEAD4, TEF3
Sequence domains: YAP binding domain
Transcriptional coactivator YAP1 Chain: L
Molecule details ›
Chain: L
Length: 41 amino acids
Theoretical weight: 4.65 KDa
Source organism: Homo sapiens
  • Canonical: P46937 (Residues: 60-100; Coverage: 8%)
Gene names: YAP1, YAP65

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 59.149Å b: 59.149Å c: 158.999Å
α: 90° β: 90° γ: 90°
R R work R free
0.219 0.218 0.242
Expression system: Escherichia coli BL21