Beta-catenin/phosphorylated E-cadherin complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 May 2001.
Explore 1I7W in 3D Show helices and sheets RCSB PDB PDBe
1I7W contains 83 α-helices and 2 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 | 153-160 | 8 | |
| α-helix | 165-180 | 16 | |
| 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 | 334-347 | 14 | |
| α-helix | 353-359 | 7 | |
| α-helix | 362-367 | 6 | |
| α-helix | 375-389 | 15 | |
| α-helix | 399-408 | 10 | |
| α-helix | 414-428 | 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 | 504-517 | 14 | |
| α-helix | 521-529 | 9 | |
| α-helix | 532-547 | 16 | |
| α-helix | 566-580 | 15 | |
| α-helix | 584-592 | 9 | |
| α-helix | 596-602 | 7 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-632 | 8 | |
| α-helix | 637-643 | 7 | |
| α-helix | 649-661 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 662-666 | 5 | |
| α-helix | 672 | 1 | |
| α-helix | 691-693 | 3 | |
| α-helix | 713-715 | 3 | |
| α-helix | 716-721 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 144-160 | 17 | |
| 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 | 353-359 | 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 | 490-496 | 7 | |
| α-helix | 504-517 | 14 | |
| α-helix | 521-529 | 9 | |
| α-helix | 532-547 | 16 | |
| α-helix | 566-580 | 15 | |
| α-helix | 584-592 | 9 | |
| α-helix | 596-602 | 7 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-633 | 9 | |
| α-helix | 637-642 | 6 | |
| α-helix | 643-645 | 3 | |
| α-helix | 649-661 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 633 | 1 | 1 |
| α-helix | 658-665 | 8 | |
| α-helix | 672-673 | 2 | |
| β-strand | 674 | 1 | 1 |
| α-helix | 691-693 | 3 | |
| α-helix | 706-710 | 5 | |
| α-helix | 713-715 | 3 | |
| α-helix | 716-721 | 6 |
| 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) |
>1I7W_1 BETA-CATENIN (chains A, C) HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQ MVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLF YAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKL IILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYK NKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPV VVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSM GGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK
>1I7W_2 EPITHELIAL-CADHERIN (chains B, D) RRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTL MSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSS ESDQDQDYDYLNEWGNRFKKLADMYGGGEDD
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Water and common crystallization additives (CL) are not listed.
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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