Solution structure of Hox homeodomain. Determined by solution NMR. Released 16 Sept 2015.
Explore 2MSY in 3D Show helices and sheets RCSB PDB PDBe
2MSY contains 3 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 18-29 | 12 | |
| α-helix | 36-45 | 10 | |
| α-helix | 50-65 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Homeobox protein Hox-C9 | A | protein | 68 | Homo sapiens | P31274 (AlphaFold model) |
>2MSY_1 Homeobox protein Hox-C9 (chains A) ANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARVLNLTERQVKIWFQNR RMKMKKMN
Structural insight into the interaction between the Hox and HMGB1 and understanding of the HMGB1-enhancing effect of Hox-DNA binding. Kim, H.H., Park, S.J., Han, J.H. et al. Biochim Biophys Acta (2015) 1854:449-459. DOI 10.1016/j.bbapap.2015.02.009 · PubMed
Other PDB entries of the same protein (UniProt P31274 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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