Crystal structure of TEAD4 in complex with YAP peptide. Determined by X-ray diffraction at 1.7 Å resolution. Released 28 Dec 2022.
Explore 8A8R in 3D Show helices and sheets RCSB PDB PDBe
8A8R contains 21 α-helices and 28 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 220 | 1 | 1 |
| β-strand | 225-238 | 14 | 1 |
| β-strand | 241-250 | 10 | 1 |
| β-strand | 264-266 | 3 | 2 |
| α-helix | 267-269 | 3 | |
| α-helix | 271-273 | 3 | |
| α-helix | 281-287 | 7 | |
| α-helix | 290-292 | 3 | |
| β-strand | 293-300 | 8 | 2 |
| β-strand | 311-322 | 12 | 1 |
| β-strand | 328-336 | 9 | 2 |
| β-strand | 339-348 | 10 | 2 |
| β-strand | 351-353 | 3 | 1 |
| β-strand | 356-365 | 10 | 1 |
| α-helix | 366-367 | 2 | |
| α-helix | 368-378 | 11 | |
| α-helix | 383-390 | 8 | |
| β-strand | 393-401 | 9 | 2 |
| β-strand | 407-417 | 11 | 2 |
| β-strand | 425-432 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 220 | 1 | 1 |
| β-strand | 225-238 | 14 | 1 |
| β-strand | 241-250 | 10 | 1 |
| α-helix | 259-261 | 3 | |
| β-strand | 264-266 | 3 | 3 |
| α-helix | 267-269 | 3 | |
| α-helix | 271-273 | 3 | |
| α-helix | 281-287 | 7 | |
| α-helix | 290-292 | 3 | |
| β-strand | 293-300 | 8 | 3 |
| β-strand | 312-322 | 11 | 1 |
| β-strand | 328-336 | 9 | 3 |
| β-strand | 339-348 | 10 | 3 |
| β-strand | 351-353 | 3 | 1 |
| β-strand | 356-365 | 10 | 1 |
| α-helix | 366-367 | 2 | |
| α-helix | 368-378 | 11 | |
| α-helix | 383-390 | 8 | |
| β-strand | 393-401 | 9 | 3 |
| β-strand | 407-417 | 11 | 3 |
| β-strand | 425-432 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 54-57 | 4 | 2 |
| α-helix | 61-73 | 13 | |
| α-helix | 86-88 | 3 | |
| α-helix | 93-95 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 54-57 | 4 | 3 |
| α-helix | 61-70 | 10 | |
| α-helix | 86-88 | 3 | |
| α-helix | 93-96 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcriptional enhancer factor TEF-3 | A, B | protein | 219 | Homo sapiens | Q15561 (AlphaFold model) |
| Isoform 7 of Transcriptional coactivator YAP1 | L, M | protein | 53 | Homo sapiens | P46937 (AlphaFold model) |
>8A8R_1 Transcriptional enhancer factor TEF-3 (chains A, B) GRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYDKFP EKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCSTKVC SFGKQVVEKVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFTI LQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE
>8A8R_2 Isoform 7 of Transcriptional coactivator YAP1 (chains L, M) XAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEX
| ID | Name | Formula | Copies |
|---|---|---|---|
| MYR | Myristic acid | C14 H28 O2 | 2 |
N-terminal beta-strand in YAP is critical for stronger binding to scalloped relative to TEAD transcription factor. Fedir, B., Yannick, M., Marco, M. et al. Protein Sci (2023) 32:e4545-e4545. DOI 10.1002/pro.4545 · PubMed
Other PDB entries of the same protein (UniProt Q15561 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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