Crystal structure of VopL C terminal domain. Determined by X-ray diffraction at 2.31 Å resolution. Released 31 Aug 2011.
Explore 3SEO in 3D Show helices and sheets RCSB PDB PDBe
3SEO contains 36 α-helices and 4 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 | 4-6 | 3 | |
| α-helix | 10-13 | 4 | |
| α-helix | 14-16 | 3 | |
| α-helix | 19-36 | 18 | |
| α-helix | 41-47 | 7 | |
| α-helix | 54-58 | 5 | |
| α-helix | 63-72 | 10 | |
| α-helix | 97-105 | 9 | |
| β-strand | 112-113 | 2 | 1 |
| β-strand | 125-126 | 2 | 1 |
| α-helix | 127-140 | 14 | |
| α-helix | 144-151 | 8 | |
| α-helix | 152-154 | 3 | |
| α-helix | 155-163 | 9 | |
| α-helix | 167-169 | 3 | |
| α-helix | 172-176 | 5 | |
| α-helix | 178-190 | 13 | |
| α-helix | 198-212 | 15 | |
| α-helix | 215-217 | 3 | |
| α-helix | 219-237 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| α-helix | 10-13 | 4 | |
| α-helix | 14-16 | 3 | |
| α-helix | 19-36 | 18 | |
| α-helix | 41-49 | 9 | |
| α-helix | 54-58 | 5 | |
| α-helix | 63-72 | 10 | |
| α-helix | 76-78 | 3 | |
| α-helix | 97-107 | 11 | |
| β-strand | 112-116 | 5 | 2 |
| β-strand | 122-126 | 5 | 2 |
| α-helix | 127-140 | 14 | |
| α-helix | 144-151 | 8 | |
| α-helix | 152-154 | 3 | |
| α-helix | 155-163 | 9 | |
| α-helix | 167-169 | 3 | |
| α-helix | 172-191 | 20 | |
| α-helix | 198-211 | 14 | |
| α-helix | 215-217 | 3 | |
| α-helix | 219-239 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| VopL C terminal domain protein | A, B | protein | 241 | Vibrio parahaemolyticus | Q87GE5 (AlphaFold model) |
>3SEO_1 VopL C terminal domain protein (chains A, B) GHMRLLSEDLFKQSPKLSEQELDELANNLADYLFQAADIDWHQVISEKTRGLTTEEMAKS EHRYVQAFCREILKYPDCYKSADVASPESPKSGGGSVIDVALKRLQTGRERLFTTTDEKG NRELKKGDAILESAINAARMAISTEEKNTILSNNVKSATFEVFCELPCMDGFAEQNGKTA FYALRAGFYSAFKNTDTAKQDITKFMKDNLQAGFSGYSYQGLTNRVAQLEAQLAALSAKL S
Mechanism of actin filament nucleation by the bacterial effector VopL. Yu, B., Cheng, H.C., Brautigam, C.A. et al. Nat Struct Mol Biol (2011) 18:1068-1074. DOI 10.1038/nsmb.2110 · PubMed
Other PDB entries of the same protein (UniProt Q87GE5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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