Crystal structure of beta-catenin in complex with alpha-helical peptide inhibitor. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Sept 2024.
Explore 8RU3 in 3D Show helices and sheets RCSB PDB PDBe
8RU3 contains 41 α-helices and 2 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 148-150 | 3 | |
| α-helix | 152-161 | 10 | |
| α-helix | 165-178 | 14 | |
| α-helix | 182-189 | 8 | |
| α-helix | 192-204 | 13 | |
| α-helix | 208-221 | 14 | |
| α-helix | 225-233 | 9 | |
| α-helix | 236-242 | 7 | |
| α-helix | 243-245 | 3 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-275 | 7 | |
| α-helix | 278-284 | 7 | |
| α-helix | 285-287 | 3 | |
| α-helix | 291-305 | 15 | |
| α-helix | 309-317 | 9 | |
| α-helix | 320-330 | 11 | |
| α-helix | 334-348 | 15 | |
| α-helix | 351-353 | 3 | |
| α-helix | 354-359 | 6 | |
| α-helix | 362-367 | 6 | |
| α-helix | 375-388 | 14 | |
| α-helix | 399-408 | 10 | |
| α-helix | 414-428 | 15 | |
| α-helix | 432-440 | 9 | |
| α-helix | 443-454 | 12 | |
| α-helix | 458-471 | 14 | |
| α-helix | 478-487 | 10 | |
| α-helix | 491-496 | 6 | |
| α-helix | 504-518 | 15 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-529 | 6 | |
| α-helix | 532-547 | 16 | |
| β-strand | 561 | 1 | 1 |
| β-strand | 564 | 1 | 1 |
| α-helix | 566-580 | 15 | |
| α-helix | 584-592 | 9 | |
| α-helix | 596-601 | 6 | |
| α-helix | 602-604 | 3 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-633 | 9 | |
| α-helix | 637-643 | 7 | |
| α-helix | 649-662 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 471-480 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Catenin beta-1 | A | protein | 534 | Homo sapiens | P35222 (AlphaFold model) |
| Axin-1 | P | protein | 14 | Homo sapiens | O15169 (AlphaFold model) |
>8RU3_1 Catenin beta-1 (chains A) GPHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRS PQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSV LFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQES KLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLT DPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNN YKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGL PVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRT SMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQ RVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSED
>8RU3_2 Axin-1 (chains P) XESILDEHLQRVWX
Structure-Based Design of Bicyclic Helical Peptides That Target the Oncogene beta-Catenin. Yeste-Vazquez, A., Paulussen, F.M., Wendt, M. et al. Angew Chem Int Ed Engl (2024) 63:e202411749-e202411749. DOI 10.1002/anie.202411749 · PubMed
Other PDB entries of the same protein (UniProt P35222 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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