Dimerization domain of Vibrio parahemolyticus VopL. Determined by X-ray diffraction at 3.1 Å resolution. Released 31 Aug 2011.
Explore 3RYL in 3D Show helices and sheets RCSB PDB PDBe
3RYL contains 26 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 | 252-256 | 5 | |
| α-helix | 262-278 | 17 | |
| α-helix | 284-292 | 9 | |
| α-helix | 297-300 | 4 | |
| α-helix | 306-312 | 7 | |
| α-helix | 313-316 | 4 | |
| α-helix | 341-349 | 9 | |
| β-strand | 360 | 1 | 1 |
| β-strand | 364 | 1 | 1 |
| α-helix | 375-384 | 10 | |
| α-helix | 387-394 | 8 | |
| α-helix | 398-407 | 10 | |
| α-helix | 415-432 | 18 | |
| α-helix | 438-440 | 3 | |
| α-helix | 441-454 | 14 | |
| α-helix | 462-474 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 252-256 | 5 | |
| α-helix | 262-278 | 17 | |
| α-helix | 306-315 | 10 | |
| α-helix | 342-346 | 5 | |
| β-strand | 360 | 1 | 2 |
| β-strand | 363 | 1 | 2 |
| α-helix | 375-383 | 9 | |
| α-helix | 387-394 | 8 | |
| α-helix | 398-406 | 9 | |
| α-helix | 410-412 | 3 | |
| α-helix | 415-433 | 19 | |
| α-helix | 438-440 | 3 | |
| α-helix | 441-454 | 14 | |
| α-helix | 462-479 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| protein VPA1370 | A, B | protein | 241 | Vibrio parahaemolyticus | Q87GE5 (AlphaFold model) |
>3RYL_1 protein VPA1370 (chains A, B) GHMRLLSEDLFKQSPKLSEQELDELANNLADYLFQAADIDWHQVISEKTRGLTTEEMAKS EHRYVQAFCREILKYPDCYKSADVASPESPKSGGGSVIDVALKRLQTGRERLFTTTDEKG NRELKKGDAILESAINAARMAISTEEKNTILSNNVKSATFEVFCELPCMDGFAEQNGKTA FYALRAGFYSAFKNTDTAKQDITKFMKDNLQAGFSGYSYQGLTNRVAQLEAQLAALSAKL S
Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Namgoong, S., Boczkowska, M., Glista, M.J. et al. Nat Struct Mol Biol (2011) 18:1060-1067. DOI 10.1038/nsmb.2109 · 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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