Smad1 crystal structure reveals the details of BMP signaling pathway. Determined by X-ray diffraction at 2.5 Å resolution. Released 12 Dec 2001.
Explore 1KHU in 3D Show helices and sheets RCSB PDB PDBe
1KHU contains 32 α-helices and 50 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 |
|---|---|---|---|
| β-strand | 272-278 | 7 | 1 |
| β-strand | 281-282 | 2 | 1 |
| β-strand | 287-288 | 2 | 1 |
| β-strand | 293-297 | 5 | 2 |
| β-strand | 308-310 | 3 | 2 |
| α-helix | 321-327 | 7 | |
| β-strand | 334-338 | 5 | 2 |
| β-strand | 342-347 | 6 | 2 |
| β-strand | 353-356 | 4 | 1 |
| α-helix | 358-363 | 6 | |
| β-strand | 372-374 | 3 | 1 |
| β-strand | 379-384 | 6 | 2 |
| α-helix | 385-393 | 9 | |
| α-helix | 400-404 | 5 | |
| α-helix | 405-410 | 6 | |
| β-strand | 411-416 | 6 | 1 |
| α-helix | 429-431 | 3 | |
| β-strand | 435-440 | 6 | 1 |
| α-helix | 441-451 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 272-278 | 7 | 3 |
| β-strand | 281-282 | 2 | 3 |
| α-helix | 285-286 | 2 | |
| β-strand | 287-288 | 2 | 3 |
| β-strand | 293-297 | 5 | 4 |
| β-strand | 308-310 | 3 | 4 |
| α-helix | 321-329 | 9 | |
| β-strand | 334-339 | 6 | 4 |
| β-strand | 342-347 | 6 | 4 |
| β-strand | 353-356 | 4 | 3 |
| α-helix | 358-364 | 7 | |
| β-strand | 371-374 | 4 | 3 |
| β-strand | 379-384 | 6 | 4 |
| α-helix | 385-395 | 11 | |
| α-helix | 396-398 | 3 | |
| α-helix | 400-404 | 5 | |
| α-helix | 405-410 | 6 | |
| β-strand | 411-416 | 6 | 3 |
| β-strand | 421 | 1 | 5 |
| β-strand | 427 | 1 | 5 |
| α-helix | 429-431 | 3 | |
| β-strand | 435-440 | 6 | 3 |
| α-helix | 441-451 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 272-278 | 7 | 6 |
| β-strand | 281-282 | 2 | 6 |
| α-helix | 285-286 | 2 | |
| β-strand | 287-288 | 2 | 6 |
| β-strand | 293-296 | 4 | 7 |
| β-strand | 308 | 1 | 7 |
| α-helix | 321-327 | 7 | |
| β-strand | 334-339 | 6 | 7 |
| β-strand | 342-347 | 6 | 7 |
| β-strand | 353-356 | 4 | 6 |
| α-helix | 358-364 | 7 | |
| β-strand | 372-374 | 3 | 6 |
| β-strand | 379-384 | 6 | 7 |
| α-helix | 385-395 | 11 | |
| α-helix | 400-405 | 6 | |
| α-helix | 408-410 | 3 | |
| β-strand | 411-416 | 6 | 6 |
| α-helix | 429-431 | 3 | |
| β-strand | 435-440 | 6 | 6 |
| α-helix | 441-453 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 272-278 | 7 | 8 |
| β-strand | 281-282 | 2 | 8 |
| α-helix | 285-286 | 2 | |
| β-strand | 287-288 | 2 | 8 |
| β-strand | 293-297 | 5 | 9 |
| β-strand | 308-310 | 3 | 9 |
| α-helix | 321-327 | 7 | |
| β-strand | 334-338 | 5 | 9 |
| β-strand | 342-347 | 6 | 9 |
| β-strand | 353-356 | 4 | 8 |
| α-helix | 358-364 | 7 | |
| β-strand | 372-374 | 3 | 8 |
| β-strand | 379-384 | 6 | 9 |
| α-helix | 385-395 | 11 | |
| α-helix | 401-404 | 4 | |
| α-helix | 405-410 | 6 | |
| β-strand | 411-416 | 6 | 8 |
| α-helix | 429-431 | 3 | |
| β-strand | 435-440 | 6 | 8 |
| α-helix | 441-451 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SMAD1 | A, B, C, D | protein | 218 | Homo sapiens | Q15797 (AlphaFold model) |
>1KHU_1 SMAD1 (chains A, B, C, D) APPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKN RFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFH PTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQ DVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
Structural basis of Smad1 activation by receptor kinase phosphorylation. Qin, B.Y., Chacko, B.M., Lam, S.S. et al. Mol Cell (2001) 8:1303-1312. DOI 10.1016/S1097-2765(01)00417-8 · PubMed
Other PDB entries of the same protein (UniProt Q15797 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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