PML-RBCC dimer. Determined by electron microscopy at 5.3 Å resolution. Released 26 Feb 2025.
Explore 8YTC in 3D Show helices and sheets RCSB PDB PDBe
8YTC contains 18 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 |
|---|---|---|---|
| α-helix | 50-53 | 4 | |
| α-helix | 80-83 | 4 | |
| α-helix | 110-122 | 13 | |
| α-helix | 127-130 | 4 | |
| α-helix | 132-137 | 6 | |
| α-helix | 150-157 | 8 | |
| α-helix | 166-169 | 4 | |
| α-helix | 175-182 | 8 | |
| β-strand | 203-204 | 2 | 1 |
| β-strand | 209-210 | 2 | 1 |
| α-helix | 214-216 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein PML | A, B | protein | 211 | Homo sapiens | P29590 (AlphaFold model) |
>8YTC_1 Protein PML (chains A, B) PASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALD NVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARP LAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSEL KCDISAEIQQRQEELDAMTQALQEQDSAFGA
Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism. Tan, Y., Li, J., Zhang, S. et al. Cell Discov (2024) 10:118-118. DOI 10.1038/s41421-024-00735-3 · PubMed
Other PDB entries of the same protein (UniProt P29590 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8YTC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.