X-ray diffraction
2.01Å resolution

TEAD4(216-434) complexed with optimized peptide 9 and myristoate (covalently bound) at 2.01A resolution: Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence


Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcriptional enhancer factor TEF-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 25.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: Q15561 (Residues: 217-434; Coverage: 50%)
Gene names: RTEF1, TCF13L1, TEAD4, TEF3
Sequence domains: YAP binding domain
Molecule details ›
Chains: C, D
Length: 17 amino acids
Theoretical weight: 2.06 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:

3 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 172.868Å b: 40.438Å c: 98.034Å
α: 90° β: 93.44° γ: 90°
R R work R free
0.218 0.217 0.244
Expression systems:
  • Escherichia coli BL21
  • Not provided