Solution structure of the MYND domain from human AML1-ETO. Determined by solution NMR. Released 19 Jun 2007.
Explore 2OD1 in 3D Show helices and sheets RCSB PDB PDBe
2OD1 contains 1 α-helix and 2 β-strands across 1 chain. 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 | 672-673 | 2 | 1 |
| β-strand | 681-682 | 2 | 1 |
| α-helix | 685-695 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein CBFA2T1 | A | protein | 60 | Homo sapiens | Q06455 (AlphaFold model) |
>2OD1_1 Protein CBFA2T1 (chains A) GSPNSGSPNSDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Liu, Y., Chen, W., Gaudet, J. et al. Cancer Cell (2007) 11:483-497. DOI 10.1016/j.ccr.2007.04.010 · PubMed
Other PDB entries of the same protein (UniProt Q06455 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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