Structure of beta-catenin with Lef-1. Determined by X-ray diffraction at 2.91 Å resolution. Released 24 Nov 2010.
Explore 3OUW in 3D Show helices and sheets RCSB PDB PDBe
3OUW contains 38 α-helices and 0 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 | 168-172 | 5 | |
| α-helix | 182-189 | 8 | |
| α-helix | 192-204 | 13 | |
| α-helix | 210-221 | 12 | |
| α-helix | 225-232 | 8 | |
| α-helix | 236-242 | 7 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-275 | 7 | |
| α-helix | 278-284 | 7 | |
| α-helix | 291-305 | 15 | |
| α-helix | 309-318 | 10 | |
| α-helix | 320-330 | 11 | |
| α-helix | 334-347 | 14 | |
| α-helix | 353-359 | 7 | |
| α-helix | 362-366 | 5 | |
| α-helix | 375-388 | 14 | |
| α-helix | 391-394 | 4 | |
| α-helix | 399-408 | 10 | |
| α-helix | 414-427 | 14 | |
| α-helix | 432-440 | 9 | |
| α-helix | 443-452 | 10 | |
| α-helix | 458-471 | 14 | |
| α-helix | 478-487 | 10 | |
| α-helix | 491-496 | 6 | |
| α-helix | 504-517 | 14 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-528 | 5 | |
| α-helix | 532-543 | 12 | |
| α-helix | 566-580 | 15 | |
| α-helix | 584-591 | 8 | |
| α-helix | 596-602 | 7 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-633 | 9 | |
| α-helix | 637-643 | 7 | |
| α-helix | 649-661 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-20 | 4 | |
| α-helix | 49-53 | 5 | |
| α-helix | 54-56 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Catenin beta-1 | A | protein | 540 | Mus musculus | Q02248 (AlphaFold model) |
| Lymphoid enhancer-binding factor 1 | B | protein | 65 | Mus musculus | P27782 (AlphaFold model) |
>3OUW_1 Catenin beta-1 (chains A) GSHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRS PQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSV LFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQES KLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLT DPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNN YKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGL PVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRT SMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQ RVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK
>3OUW_2 Lymphoid enhancer-binding factor 1 (chains B) GAMPQLSGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNE SEIIP
Biochemical and structural characterization of beta-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1. Sun, J., Weis, W.I. J Mol Biol (2011) 405:519-530. DOI 10.1016/j.jmb.2010.11.010 · PubMed
Other PDB entries of the same protein (UniProt Q02248 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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