Beta-catenin/e-cadherin complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 16 May 2001.
Explore 1I7X in 3D Show helices and sheets RCSB PDB PDBe
1I7X contains 84 α-helices and 8 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 |
|---|---|---|---|
| α-helix | 142-150 | 9 | |
| α-helix | 153-161 | 9 | |
| α-helix | 165-180 | 16 | |
| α-helix | 182-188 | 7 | |
| 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 | 278-285 | 8 | |
| α-helix | 291-305 | 15 | |
| α-helix | 309-317 | 9 | |
| α-helix | 320-330 | 11 | |
| α-helix | 334-348 | 15 | |
| α-helix | 353-359 | 7 | |
| α-helix | 362-367 | 6 | |
| α-helix | 375-388 | 14 | |
| α-helix | 389-392 | 4 | |
| 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 | 490-496 | 7 | |
| α-helix | 504-517 | 14 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-528 | 5 | |
| α-helix | 532-549 | 18 | |
| β-strand | 561 | 1 | 1 |
| β-strand | 564 | 1 | 1 |
| α-helix | 566-580 | 15 | |
| α-helix | 584-592 | 9 | |
| α-helix | 596-603 | 8 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-634 | 10 | |
| α-helix | 637-642 | 6 | |
| α-helix | 643-645 | 3 | |
| α-helix | 649-663 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 630-633 | 4 | 2 |
| α-helix | 650-652 | 3 | |
| α-helix | 653-666 | 14 | |
| α-helix | 672-673 | 2 | |
| β-strand | 674-677 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 137-160 | 24 | |
| 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 | 236-243 | 8 | |
| 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 | 353-360 | 8 | |
| 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 | 490-496 | 7 | |
| α-helix | 504-518 | 15 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-529 | 6 | |
| α-helix | 532-546 | 15 | |
| β-strand | 561 | 1 | 3 |
| β-strand | 564 | 1 | 3 |
| α-helix | 566-580 | 15 | |
| α-helix | 584-591 | 8 | |
| α-helix | 596-599 | 4 | |
| α-helix | 600-603 | 4 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-632 | 8 | |
| α-helix | 637-642 | 6 | |
| α-helix | 649-662 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 632-633 | 2 | 4 |
| α-helix | 656-658 | 3 | |
| α-helix | 662-665 | 4 | |
| α-helix | 673 | 1 | |
| β-strand | 674-675 | 2 | 4 |
| α-helix | 706-708 | 3 | |
| α-helix | 713-715 | 3 | |
| α-helix | 716-722 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-catenin | A, C | protein | 538 | Mus musculus | Q02248 (AlphaFold model) |
| Epithelial-cadherin | B, D | protein | 151 | Mus musculus | P09803 (AlphaFold model) |
>1I7X_1 BETA-CATENIN (chains A, C) HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQ MVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLF YAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKL IILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYK NKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPV VVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSM GGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK
>1I7X_2 EPITHELIAL-CADHERIN (chains B, D) RRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTL MSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSS ESDQDQDYDYLNEWGNRFKKLADMYGGGEDD
The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. Huber, A.H., Weis, W.I. Cell (2001) 105:391-402. DOI 10.1016/S0092-8674(01)00330-0 · 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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