Crystal structure of human SMAD2-MAN1 complex. Determined by X-ray diffraction at 2.79 Å resolution. Released 10 Oct 2018.
Explore 5ZOJ in 3D Show helices and sheets RCSB PDB PDBe
5ZOJ contains 35 α-helices and 50 β-strands across 5 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 | 275-281 | 7 | 1 |
| β-strand | 284-285 | 2 | 1 |
| α-helix | 288-289 | 2 | |
| β-strand | 290-291 | 2 | 1 |
| β-strand | 296-300 | 5 | 2 |
| β-strand | 310-312 | 3 | 2 |
| α-helix | 323-330 | 8 | |
| β-strand | 336-341 | 6 | 2 |
| β-strand | 344-349 | 6 | 2 |
| β-strand | 355-358 | 4 | 1 |
| α-helix | 360-366 | 7 | |
| β-strand | 374-376 | 3 | 1 |
| β-strand | 381-386 | 6 | 2 |
| α-helix | 387-398 | 12 | |
| α-helix | 402-406 | 5 | |
| α-helix | 407-412 | 6 | |
| β-strand | 413-418 | 6 | 1 |
| α-helix | 431-433 | 3 | |
| β-strand | 437-442 | 6 | 1 |
| α-helix | 443-455 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 275-281 | 7 | 3 |
| β-strand | 284-285 | 2 | 3 |
| α-helix | 288-289 | 2 | |
| β-strand | 290-292 | 3 | 3 |
| β-strand | 296-300 | 5 | 4 |
| β-strand | 310-312 | 3 | 4 |
| α-helix | 323-330 | 8 | |
| β-strand | 336-341 | 6 | 4 |
| β-strand | 344-349 | 6 | 4 |
| β-strand | 355-358 | 4 | 3 |
| α-helix | 360-366 | 7 | |
| β-strand | 374-376 | 3 | 3 |
| β-strand | 381-386 | 6 | 4 |
| α-helix | 387-398 | 12 | |
| α-helix | 402-406 | 5 | |
| α-helix | 407-410 | 4 | |
| β-strand | 413-418 | 6 | 3 |
| α-helix | 431-433 | 3 | |
| β-strand | 437-442 | 6 | 3 |
| α-helix | 443-455 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 275-281 | 7 | 5 |
| β-strand | 284-285 | 2 | 5 |
| α-helix | 288-289 | 2 | |
| β-strand | 290-292 | 3 | 5 |
| β-strand | 296-300 | 5 | 6 |
| β-strand | 310-312 | 3 | 6 |
| α-helix | 323-330 | 8 | |
| β-strand | 336-341 | 6 | 6 |
| β-strand | 344-349 | 6 | 6 |
| β-strand | 355-358 | 4 | 5 |
| α-helix | 360-365 | 6 | |
| β-strand | 374-376 | 3 | 5 |
| β-strand | 381-386 | 6 | 6 |
| α-helix | 387-397 | 11 | |
| α-helix | 398-400 | 3 | |
| α-helix | 402-406 | 5 | |
| α-helix | 407-411 | 5 | |
| β-strand | 413-418 | 6 | 5 |
| α-helix | 431-433 | 3 | |
| β-strand | 437-442 | 6 | 5 |
| α-helix | 443-455 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 765-768 | 4 | 7 |
| β-strand | 785-789 | 5 | 8 |
| α-helix | 794-796 | 3 | |
| α-helix | 803-813 | 11 | |
| 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 | 859-861 | 3 | 7 |
| β-strand | 862-865 | 4 | 8 |
| α-helix | 868-874 | 7 | |
| α-helix | 876-880 | 5 | |
| α-helix | 884-885 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 765-768 | 4 | 9 |
| β-strand | 785-789 | 5 | 10 |
| α-helix | 794-796 | 3 | |
| α-helix | 802-813 | 12 | |
| β-strand | 820-825 | 6 | 10 |
| β-strand | 834-838 | 5 | 10 |
| α-helix | 841-851 | 11 | |
| β-strand | 854-856 | 3 | 9 |
| β-strand | 859-861 | 3 | 9 |
| β-strand | 862-865 | 4 | 10 |
| α-helix | 884-885 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mothers against decapentaplegic homolog 2 | A, B, C | protein | 200 | Homo sapiens | Q15796 (AlphaFold model) |
| Inner nuclear membrane protein Man1 | D, E | protein | 132 | Homo sapiens | Q9Y2U8 (AlphaFold model) |
>5ZOJ_1 Mothers against decapentaplegic homolog 2 (chains A, B, C) GPGDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSN VNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPP GCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWI ELHLNGPLQWLDKVLTQMGS
>5ZOJ_2 Inner nuclear membrane protein Man1 (chains D, E) 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 Q15796 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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