Crystal structure of the MLL5 PHD finger in complex with H3K4me3. Determined by X-ray diffraction at 1.48 Å resolution. Released 26 Jun 2013.
Explore 4L58 in 3D Show helices and sheets RCSB PDB PDBe
4L58 contains 2 α-helices and 4 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 |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| β-strand | 16-18 | 3 | 1 |
| β-strand | 25-27 | 3 | 1 |
| α-helix | 28-31 | 4 | |
| α-helix | 54-62 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone-lysine N-methyltransferase MLL5 | A | protein | 69 | Homo sapiens | Q8IZD2 (AlphaFold model) |
| Histone H3 peptide | B | protein | 12 | Homo sapiens | P84243 (AlphaFold model) |
>4L58_1 Histone-lysine N-methyltransferase MLL5 (chains A) GSHMDVTRCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERCQPRNLDKER AVLLQRRKR
>4L58_2 Histone H3 peptide (chains B) ARTKQTARKSTG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Molecular basis for chromatin binding and regulation of MLL5. Ali, M., Rincon-Arano, H., Zhao, W. et al. Proc Natl Acad Sci U S A (2013) 110:11296-11301. DOI 10.1073/pnas.1310156110 · PubMed
Other PDB entries of the same protein (UniProt Q8IZD2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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