Cystal structure of the Dpy30 for MLL/SET1 COMPASS H3K4 trimethylation. Determined by X-ray diffraction at 2.12 Å resolution. Released 7 Oct 2015.
Explore 4RTA in 3D Show helices and sheets RCSB PDB PDBe
4RTA contains 8 α-helices and 0 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 | 53-60 | 8 | |
| α-helix | 62-75 | 14 | |
| α-helix | 80-95 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-34 | 4 | |
| α-helix | 48-50 | 3 | |
| α-helix | 53-60 | 8 | |
| α-helix | 62-75 | 14 | |
| α-helix | 80-95 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein dpy-30 homolog | A, B | protein | 106 | Homo sapiens | Q9C005 (AlphaFold model) |
>4RTA_1 Protein dpy-30 homolog (chains A, B) MEPEQMLEGQTQVAENPHSEYGLTDNVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQT VVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRNLERPHRD
Structural implications of Dpy30 oligomerization for MLL/SET1 COMPASS H3K4 trimethylation. Zhang, H., Li, M., Gao, Y. et al. Protein Cell (2015) 6:147-151. DOI 10.1007/s13238-014-0127-z · PubMed
Other PDB entries of the same protein (UniProt Q9C005 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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