Crystal structure of beta-catenin and htcf-4. Determined by X-ray diffraction at 1.9 Å resolution. Released 5 Dec 2001.
Explore 1JDH in 3D Show helices and sheets RCSB PDB PDBe
1JDH contains 42 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 | 152-160 | 9 | |
| α-helix | 165-179 | 15 | |
| α-helix | 182-189 | 8 | |
| α-helix | 192-204 | 13 | |
| α-helix | 208-221 | 14 | |
| α-helix | 225-233 | 9 | |
| α-helix | 236-243 | 8 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-276 | 8 | |
| 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 | 334-347 | 14 | |
| α-helix | 353-359 | 7 | |
| α-helix | 362-367 | 6 | |
| α-helix | 375-389 | 15 | |
| α-helix | 399-408 | 10 | |
| α-helix | 414-427 | 14 | |
| 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 | 504-517 | 14 | |
| 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 | 637-642 | 6 | |
| α-helix | 643-645 | 3 | |
| α-helix | 649-662 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-16 | 3 | |
| α-helix | 22-31 | 10 | |
| α-helix | 33-35 | 3 | |
| α-helix | 38-48 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-catenin | A | protein | 529 | Homo sapiens | P35222 (AlphaFold model) |
| hTcf-4 | B | protein | 38 | Homo sapiens | Q9NQB0 (AlphaFold model) |
>1JDH_1 BETA-CATENIN (chains A) AVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQM VSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFY AITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLI ILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPS QRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKN KMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVV VKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMG GTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVA AGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMS
>1JDH_2 hTcf-4 (chains B) LGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLV
Tcf4 can specifically recognize beta-catenin using alternative conformations. Graham, T.A., Ferkey, D.M., Mao, F. et al. Nat Struct Biol (2001) 8:1048-1052. DOI 10.1038/nsb718 · 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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