Crystal Structure of the Sugar Recognizing SCF Ubiquitin Ligase at 1.7 Resolution. Determined by X-ray diffraction at 1.7 Å resolution. Released 14 Oct 2008.
Explore 2RJ2 in 3D Show helices and sheets RCSB PDB PDBe
2RJ2 contains 3 α-helices and 11 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 | 116-123 | 8 | |
| β-strand | 141-145 | 5 | 1 |
| β-strand | 151-154 | 4 | 2 |
| β-strand | 171-174 | 4 | 2 |
| β-strand | 180-187 | 8 | 1 |
| α-helix | 195-196 | 2 | |
| α-helix | 197-201 | 5 | |
| β-strand | 204-212 | 9 | 2 |
| β-strand | 219-229 | 11 | 1 |
| β-strand | 234-239 | 6 | 1 |
| β-strand | 243-244 | 2 | 1 |
| β-strand | 252-258 | 7 | 2 |
| β-strand | 265-276 | 12 | 1 |
| β-strand | 287-296 | 10 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| F-box only protein 2 | A | protein | 185 | Mus musculus | Q80UW2 (AlphaFold model) |
>2RJ2_1 F-box only protein 2 (chains A) GSHMFYFLSKRRRNLLRNPCGEEDLEGWSDVEHGGDGWKVEELPGDGNVEFTQDDSVKKY FASSFEWCRKAQVIDLQAEGYWEELLDTTQPAIVVKDWYSGRTDAGSLYELTVRLLSENE DVLAEFATGQVAVPEDGSWMEISHTFIDYGPGVRFVRFEHGGQDSVYWKGWFGARVTNSS VWVEP
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 1 |
Water and common crystallization additives (CL) are not listed.
Crystal Structure of the Sugar Recognizing SCF Ubiquitin Ligase at 1.7 Resolution. Vaijayanthimala, S., Velmurugan, D., Mizushima, T. et al. To be published.
Other PDB entries of the same protein (UniProt Q80UW2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2RJ2 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.