Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase. Determined by X-ray diffraction at 3.52 Å resolution. Released 20 Mar 2007.
Explore 2E32 in 3D Show helices and sheets RCSB PDB PDBe
2E32 contains 31 α-helices and 31 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 | 56-63 | 8 | |
| α-helix | 68-70 | 3 | |
| α-helix | 71-75 | 5 | |
| α-helix | 76-78 | 3 | |
| α-helix | 80-86 | 7 | |
| α-helix | 89-98 | 10 | |
| α-helix | 114-123 | 10 | |
| β-strand | 141-145 | 5 | 1 |
| β-strand | 152-154 | 3 | 2 |
| β-strand | 157 | 1 | 3 |
| β-strand | 160 | 1 | 3 |
| α-helix | 161-163 | 3 | |
| β-strand | 171-174 | 4 | 2 |
| β-strand | 180-187 | 8 | 1 |
| α-helix | 195-198 | 4 | |
| α-helix | 203 | 1 | |
| β-strand | 204-212 | 9 | 2 |
| β-strand | 219-229 | 11 | 1 |
| β-strand | 233-245 | 13 | 1 |
| β-strand | 251-258 | 8 | 2 |
| β-strand | 265-276 | 12 | 1 |
| β-strand | 287-296 | 10 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 4 |
| β-strand | 13-16 | 4 | 4 |
| α-helix | 25-31 | 7 | |
| β-strand | 44-46 | 3 | 4 |
| α-helix | 52-64 | 13 | |
| α-helix | 87-92 | 6 | |
| α-helix | 97-110 | 14 | |
| α-helix | 113-127 | 15 | |
| α-helix | 132-138 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-64 | 9 | |
| α-helix | 68-73 | 6 | |
| α-helix | 75-77 | 3 | |
| α-helix | 80-86 | 7 | |
| α-helix | 89-98 | 10 | |
| α-helix | 114-123 | 10 | |
| β-strand | 141-145 | 5 | 5 |
| β-strand | 152-154 | 3 | 6 |
| β-strand | 157 | 1 | 7 |
| β-strand | 160 | 1 | 7 |
| α-helix | 161-163 | 3 | |
| β-strand | 171-175 | 5 | 6 |
| β-strand | 180-187 | 8 | 5 |
| α-helix | 195-200 | 6 | |
| α-helix | 203 | 1 | |
| β-strand | 204-212 | 9 | 6 |
| β-strand | 219-229 | 11 | 5 |
| β-strand | 233-239 | 7 | 5 |
| β-strand | 243-245 | 3 | 5 |
| β-strand | 251-258 | 8 | 6 |
| β-strand | 265-276 | 12 | 5 |
| β-strand | 285-296 | 12 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| F-box only protein 2 | A, C | protein | 297 | Mus musculus | Q80UW2 (AlphaFold model) |
| S-phase kinase-associated protein 1A | B, D | protein | 166 | Homo sapiens | P63208 (AlphaFold model) |
>2E32_1 F-box only protein 2 (chains A, C) MDGDGDPESVSHPEEASPEEQPEEAGAEASAEEEQLREAEEEEEAEAVEYLAELPEPLLL RVLAELPATELVQACRLVCLRWKELVDGAPLWLLKCQQEGLVPEGSADEERDHWQQFYFL SKRRRNLLRNPCGEEDLEGWSDVEHGGDGWKVEELPGDNGVEFTQDDSVKKYFASSFEWC RKAQVIDLQAEGYWEELLDTTQPAIVVKDWYSGRTDAGSLYELTVRLLSENEDVLAEFAT GQVAVPEDGSWMEISHTFIDYGPGVRFVRFEHGGQDSVYWKGWFGARVTNSSVWVEP
>2E32_2 S-phase kinase-associated protein 1A (chains B, D) GPHMPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKK VIQWCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLD VTCKTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
Structural basis for the selection of glycosylated substrates by SCFFbs1 ubiquitin ligase. Mizushima, T., Yoshida, Y., Kumanomidou, T. et al. Proc Natl Acad Sci U S A (2007) 104:5777-5781. DOI 10.1073/pnas.0610312104 · PubMed
Other PDB entries of the same protein (UniProt Q80UW2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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