Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination. Determined by X-ray diffraction at 2.67 Å resolution. Released 19 Jun 2007.
Explore 2P63 in 3D Show helices and sheets RCSB PDB PDBe
2P63 contains 15 α-helices and 0 β-strands across 4 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 | 228-234 | 7 | |
| α-helix | 235-237 | 3 | |
| α-helix | 242-253 | 12 | |
| α-helix | 256-271 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 228-235 | 8 | |
| α-helix | 240-242 | 3 | |
| α-helix | 246-253 | 8 | |
| α-helix | 256-269 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 228-236 | 9 | |
| α-helix | 242-252 | 11 | |
| α-helix | 256-270 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 228-236 | 9 | |
| α-helix | 240-243 | 4 | |
| α-helix | 246-252 | 7 | |
| α-helix | 256-271 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division control protein 4 | A, B, C, D | protein | 56 | Saccharomyces cerevisiae | P07834 (AlphaFold model) |
>2P63_1 Cell division control protein 4 (chains A, B, C, D) GAMGSPEYLSDEIFSAINNNLPHAYFKNLLFRLVANMDRSELSDLGTLIKDNLKRD
Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination. Tang, X., Orlicky, S., Lin, Z. et al. Cell (2007) 129:1165-1176. DOI 10.1016/j.cell.2007.04.042 · PubMed
Other PDB entries of the same protein (UniProt P07834 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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