Crystal structure of stabilised vimentin coil2 fragment. Determined by X-ray diffraction at 2.3 Å resolution. Released 1 Feb 2012.
Explore 3TRT in 3D Show helices and sheets RCSB PDB PDBe
3TRT contains 3 α-helices and 0 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 | 266-334 | 69 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 266-303 | 38 | |
| α-helix | 306-333 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vimentin | A, B | protein | 77 | Homo sapiens | P08670 (AlphaFold model) |
>3TRT_1 Vimentin (chains A, B) GGSKPDCTAAMRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTE YRRQVQSLTMEVDALKG
Stabilization of vimentin coil2 fragment via an engineered disulfide. Chernyatina, A.A., Strelkov, S.V. J Struct Biol (2012) 177:46-53. DOI 10.1016/j.jsb.2011.11.014 · PubMed
Other PDB entries of the same protein (UniProt P08670 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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