Structure of Dido PHD domain. Determined by solution NMR. Released 7 Aug 2013.
Explore 2M3H in 3D Show helices and sheets RCSB PDB PDBe
2M3H contains 2 α-helices 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 | 21-24 | 4 | 1 |
| β-strand | 29-32 | 4 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-49 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Death-inducer obliterator 1 | A | protein | 61 | Homo sapiens | Q9BTC0 (AlphaFold model) |
>2M3H_1 Death-inducer obliterator 1 (chains A) GSMDPNALYCICRQPHNNRFMICCDRCEEWFHGDCVGISEARGRLLERNGEDYICPNCTI L
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3. Santiveri, C.M., Garcia-Mayoral, M.F., Perez-Canadillas, J.M. et al. J Biomol NMR (2013) 56:183-190. DOI 10.1007/s10858-013-9726-x · PubMed
Other PDB entries of the same protein (UniProt Q9BTC0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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