Structure of UHRF1 in complex with histone tail. Determined by X-ray diffraction at 1.41 Å resolution. Released 25 Jan 2012.
Explore 3ASL in 3D Show helices and sheets RCSB PDB PDBe
3ASL contains 3 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 | 318 | 1 | 1 |
| α-helix | 327-329 | 3 | |
| β-strand | 330-332 | 3 | 1 |
| α-helix | 333 | 1 | |
| β-strand | 339-341 | 3 | 1 |
| α-helix | 342-344 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase UHRF1 | A | protein | 70 | Homo sapiens | Q96T88 (AlphaFold model) |
| Histone H3.3 | B | protein | 11 | Homo sapiens | P68431 (AlphaFold model) |
>3ASL_1 E3 ubiquitin-protein ligase UHRF1 (chains A) SGPSCKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECDMAFHIYCLDPPLSSVPSEDE WYCPECRNDA
>3ASL_2 Histone H3.3 (chains B) ARTKQTARKST
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (EDO) are not listed.
Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1. Arita, K., Isogai, S., Oda, T. et al. Proc Natl Acad Sci U S A (2012) 109:12950-12955. DOI 10.1073/pnas.1203701109 · PubMed
Other PDB entries of the same protein (UniProt Q96T88 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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