Crystal structure of Smad3-MH1 bound to DNA at 2.4 A resolution. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Mar 2004.
Explore 1OZJ in 3D Show helices and sheets RCSB PDB PDBe
1OZJ contains 17 α-helices and 12 β-strands across 2 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 | 10-16 | 7 | |
| α-helix | 25-44 | 20 | |
| α-helix | 48-57 | 10 | |
| α-helix | 63-64 | 2 | |
| β-strand | 66-68 | 3 | 1 |
| α-helix | 69-70 | 2 | |
| β-strand | 75-77 | 3 | 2 |
| β-strand | 80-82 | 3 | 2 |
| α-helix | 84-92 | 9 | |
| α-helix | 100-102 | 3 | |
| β-strand | 103-105 | 3 | 3 |
| α-helix | 113-115 | 3 | |
| β-strand | 119-121 | 3 | 1 |
| α-helix | 124-126 | 3 | |
| β-strand | 127-129 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-17 | 8 | |
| α-helix | 26-44 | 19 | |
| α-helix | 48-57 | 10 | |
| β-strand | 66-68 | 3 | 4 |
| α-helix | 69-70 | 2 | |
| β-strand | 75-77 | 3 | 5 |
| β-strand | 80-82 | 3 | 5 |
| α-helix | 84-92 | 9 | |
| α-helix | 100-102 | 3 | |
| β-strand | 103-105 | 3 | 6 |
| α-helix | 113-115 | 3 | |
| β-strand | 119-121 | 3 | 4 |
| α-helix | 124-126 | 3 | |
| β-strand | 127-129 | 3 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Smad binding element | C | DNA | 15 | ||
| Smad binding element | D | DNA | 15 | ||
| Smad 3 | A, B | protein | 144 | Homo sapiens | P84022 (AlphaFold model) |
>1OZJ_1 Smad binding element (chains C) TCAGTCTAGACATAC
>1OZJ_2 Smad binding element (chains D) GTATGTCTAGACTGA
>1OZJ_3 SMAD 3 (chains A, B) MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNV NTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEV CVNPYHYQRVETPVLPPVLVPRHT
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Features of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA binding. Chai, J., Wu, J.-W., Yan, N. et al. J Biol Chem (2003) 278:20327-20331. DOI 10.1074/jbc.C300134200 · PubMed
Other PDB entries of the same protein (UniProt P84022 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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