Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI. Determined by X-ray diffraction at 2.96 Å resolution. Released 27 Mar 2013.
Explore 3W31 in 3D Show helices and sheets RCSB PDB PDBe
3W31 contains 24 α-helices and 17 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 | 24-28 | 5 | |
| α-helix | 38-53 | 16 | |
| α-helix | 62-73 | 12 | |
| β-strand | 79 | 1 | 1 |
| α-helix | 80-83 | 4 | |
| α-helix | 84-89 | 6 | |
| α-helix | 91-98 | 8 | |
| α-helix | 99-101 | 3 | |
| β-strand | 107-108 | 2 | 2 |
| α-helix | 109-110 | 2 | |
| β-strand | 114 | 1 | 3 |
| α-helix | 115-122 | 8 | |
| α-helix | 124-127 | 4 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 145-151 | 7 | 2 |
| β-strand | 156-159 | 4 | 2 |
| α-helix | 174-176 | 3 | |
| α-helix | 179 | 1 | |
| β-strand | 180 | 1 | 3 |
| α-helix | 181-182 | 2 | |
| β-strand | 186-190 | 5 | 2 |
| α-helix | 194-201 | 8 | |
| α-helix | 204-207 | 4 | |
| α-helix | 210 | 1 | |
| β-strand | 211 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-15 | 11 | |
| α-helix | 19-20 | 2 | |
| β-strand | 23-27 | 5 | 4 |
| β-strand | 34-40 | 7 | 4 |
| α-helix | 41-42 | 2 | |
| β-strand | 51-57 | 7 | 4 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-71 | 4 | 4 |
| β-strand | 77 | 1 | 5 |
| β-strand | 80 | 1 | 5 |
| β-strand | 85 | 1 | 4 |
| β-strand | 86 | 1 | 5 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-113 | 13 | |
| α-helix | 124-130 | 7 | |
| α-helix | 133-146 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ORF169b | A | protein | 220 | Shigella flexneri | Q8VSD5 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 N | B | protein | 155 | Homo sapiens | P61088 (AlphaFold model) |
>3W31_1 ORF169b (chains A) GPLGSPEFMINGVSLQGTAGYEAHTEEGNVNVKKLLESLNSKSLGDMDKDSELAATLQKM INPSGGDGNASGCALHACMAMLGYGVREAPVPNEISEYMTGFFHRHLEQIDSEGIVSHPN ETYSKFRERIAENILQNTSKGSVVMISIEQATHWIAGFNDGEKIMFLDVQTGKGFNLYDP VEKSPDAFVDENSSVQVIHVSDQEFDHYANSSSWKSKRLC
>3W31_2 Ubiquitin-conjugating enzyme E2 N (chains B) GSHMAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELF LPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNP DDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI
Structural basis for the recognition of Ubc13 by the Shigella flexneri effector OspI. Nishide, A., Kim, M., Takagi, K. et al. J Mol Biol (2013) 425:2623-2631. DOI 10.1016/j.jmb.2013.02.037 · PubMed
Other PDB entries of the same protein (UniProt Q8VSD5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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