Crystal structure of human SMAD1-MAN1 complex. Determined by X-ray diffraction at 2.85 Å resolution. Released 17 Oct 2018.
Explore 5ZOK in 3D Show helices and sheets RCSB PDB PDBe
5ZOK contains 28 α-helices and 36 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 | 281-288 | 8 | 1 |
| β-strand | 293-297 | 5 | 2 |
| β-strand | 308-310 | 3 | 2 |
| α-helix | 321-327 | 7 | |
| β-strand | 334-339 | 6 | 2 |
| β-strand | 342-347 | 6 | 2 |
| β-strand | 353-356 | 4 | 1 |
| α-helix | 358-364 | 7 | |
| α-helix | 370-371 | 2 | |
| β-strand | 372-374 | 3 | 1 |
| β-strand | 379-384 | 6 | 2 |
| 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 | 1 |
| α-helix | 429-431 | 3 | |
| β-strand | 435-440 | 6 | 1 |
| α-helix | 441-451 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 765-768 | 4 | 3 |
| α-helix | 774-776 | 3 | |
| β-strand | 785-788 | 4 | 4 |
| α-helix | 794-796 | 3 | |
| α-helix | 802-813 | 12 | |
| β-strand | 820-825 | 6 | 4 |
| β-strand | 834-838 | 5 | 4 |
| α-helix | 841-851 | 11 | |
| β-strand | 854-856 | 3 | 3 |
| β-strand | 859-861 | 3 | 3 |
| β-strand | 863-865 | 3 | 4 |
| α-helix | 868-874 | 7 | |
| α-helix | 876-879 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 272-278 | 7 | 5 |
| β-strand | 281-288 | 8 | 5 |
| β-strand | 293-297 | 5 | 6 |
| β-strand | 308-310 | 3 | 6 |
| α-helix | 321-328 | 8 | |
| β-strand | 334-339 | 6 | 6 |
| β-strand | 342-347 | 6 | 6 |
| β-strand | 353-357 | 5 | 5 |
| α-helix | 358-364 | 7 | |
| β-strand | 372-374 | 3 | 5 |
| β-strand | 379-384 | 6 | 6 |
| 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 | 5 |
| α-helix | 429-431 | 3 | |
| β-strand | 435-440 | 6 | 5 |
| α-helix | 441-451 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 765-768 | 4 | 7 |
| β-strand | 785-789 | 5 | 8 |
| α-helix | 794-796 | 3 | |
| α-helix | 802-813 | 12 | |
| β-strand | 820-825 | 6 | 8 |
| β-strand | 834-838 | 5 | 8 |
| α-helix | 841-851 | 11 | |
| β-strand | 854-856 | 3 | 7 |
| β-strand | 859-860 | 2 | 7 |
| β-strand | 862-866 | 5 | 8 |
| α-helix | 868-874 | 7 | |
| α-helix | 876-879 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mothers against decapentaplegic homolog 1 | A, C | protein | 209 | Homo sapiens | Q15797 (AlphaFold model) |
| Inner nuclear membrane protein Man1 | B, D | protein | 132 | Homo sapiens | Q9Y2U8 (AlphaFold model) |
>5ZOK_1 Mothers against decapentaplegic homolog 1 (chains A, C) GPDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSN VNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPS GCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWI EIHLHGPLQWLDKVLTQMGSPHNPISEVE
>5ZOK_2 Inner nuclear membrane protein Man1 (chains B, D) GPGSKVWQGQAFHLDRRNSPPNSLTPCLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDND GIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVKYLRLDRYHHRFPQA LTSNTPLKPSNK
Structural basis for receptor-regulated SMAD recognition by MAN1. Miyazono, K.I., Ohno, Y., Wada, H. et al. Nucleic Acids Res (2018) 46:12139-12153. DOI 10.1093/nar/gky925 · 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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