Crystal structure of Protein Scalloped in complex with YAP peptide. Determined by X-ray diffraction at 1.47 Å resolution. Released 28 Dec 2022.
Explore 8A8Q in 3D Show helices and sheets RCSB PDB PDBe
8A8Q contains 25 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 | 226 | 1 | 1 |
| β-strand | 230-243 | 14 | 1 |
| β-strand | 246-255 | 10 | 1 |
| α-helix | 263-266 | 4 | |
| β-strand | 267-270 | 4 | 2 |
| α-helix | 271-273 | 3 | |
| α-helix | 275-277 | 3 | |
| α-helix | 285-291 | 7 | |
| α-helix | 294-296 | 3 | |
| β-strand | 297-304 | 8 | 2 |
| β-strand | 319-328 | 10 | 1 |
| β-strand | 334-342 | 9 | 2 |
| β-strand | 345-354 | 10 | 2 |
| β-strand | 357-359 | 3 | 1 |
| β-strand | 362-371 | 10 | 1 |
| α-helix | 372-373 | 2 | |
| α-helix | 374-384 | 11 | |
| α-helix | 389-396 | 8 | |
| β-strand | 399-407 | 9 | 2 |
| β-strand | 413-423 | 11 | 2 |
| α-helix | 424-425 | 2 | |
| β-strand | 431-438 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 226 | 1 | 3 |
| β-strand | 230-243 | 14 | 3 |
| β-strand | 246-255 | 10 | 3 |
| β-strand | 267-270 | 4 | 2 |
| α-helix | 271-273 | 3 | |
| α-helix | 275-277 | 3 | |
| α-helix | 285-291 | 7 | |
| α-helix | 294-296 | 3 | |
| β-strand | 297-304 | 8 | 2 |
| β-strand | 319-328 | 10 | 3 |
| β-strand | 334-342 | 9 | 2 |
| β-strand | 345-354 | 10 | 2 |
| β-strand | 357-359 | 3 | 3 |
| β-strand | 362-371 | 10 | 3 |
| α-helix | 372-373 | 2 | |
| α-helix | 374-384 | 11 | |
| α-helix | 389-396 | 8 | |
| β-strand | 399-407 | 9 | 2 |
| β-strand | 413-423 | 11 | 2 |
| α-helix | 424-425 | 2 | |
| β-strand | 431-438 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 52-57 | 6 | 2 |
| α-helix | 61-73 | 13 | |
| α-helix | 83-85 | 3 | |
| α-helix | 86-88 | 3 | |
| α-helix | 93-96 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein scalloped | A, B | protein | 219 | Drosophila melanogaster | P30052 (AlphaFold model) |
| Isoform 7 of Transcriptional coactivator YAP1 | C, D | protein | 51 | Homo sapiens | P46937 (AlphaFold model) |
>8A8Q_1 Protein scalloped (chains A, B) GRAIATHKFRLLEFTAFMEIQRDEIYHRHLFVQLGGKPSFSDPLLETVDIRQIFDKFPEK SGGLKDLYEKGPQNAFYLVKCWADLNTDLTTGSETGDFYGVTSQYESNENVVLVCSTIVC SFGKQVVEXVESEYSRLENNRYVYRIQRSPMCEYMINFIQKLKNLPERYMMNSVLENFTI LQVMRARETQETLLCIAYVFEVAAQNSGTTHHIYRLIKE
>8A8Q_2 Isoform 7 of Transcriptional coactivator YAP1 (chains C, D) XGHQIVHVRGDSETDLEALFNAVLNPKTANVPQTVPLRLRKLPDSFFKPPX
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 P30052 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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