Human vinculin (head domain, Vh1, residues 1-258) in complex with Shigella's IpaA vinculin binding site (residues 602-633). Determined by X-ray diffraction at 2.72 Å resolution. Released 14 Nov 2006.
Explore 2GWW in 3D Show helices and sheets RCSB PDB PDBe
2GWW contains 11 α-helices and 2 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 |
|---|---|---|---|
| β-strand | 6 | 1 | 1 |
| α-helix | 7-28 | 22 | |
| α-helix | 36-39 | 4 | |
| α-helix | 43-64 | 22 | |
| α-helix | 68-97 | 30 | |
| α-helix | 102-147 | 46 | |
| α-helix | 148-150 | 3 | |
| α-helix | 154-179 | 26 | |
| β-strand | 182 | 1 | 1 |
| α-helix | 185-216 | 32 | |
| α-helix | 224-249 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 611-627 | 17 | |
| α-helix | 628-630 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| vinculin | A | protein | 266 | Homo sapiens | P18206 (AlphaFold model) |
| IpaA | B | protein | 30 | Shigella flexneri | P18010 (AlphaFold model) |
>2GWW_1 vinculin (chains A) MEHHHHHHMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVS NLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGS RGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMA KMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNF TVEKMSAEINEIIRVLQLTSWDEDAW
>2GWW_2 IpaA (chains B) NNDITAENNNIYKAAKDVTTSLSKVLKNIN
Shigella applies molecular mimicry to subvert vinculin and invade host cells. Izard, T., Tran Van Nhieu, G., Bois, P.R. J Cell Biol (2006) 175:465-475. DOI 10.1083/jcb.200605091 · PubMed
Other PDB entries of the same protein (UniProt P18206 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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