Crystal structure of vimentin coil1B fragment. Determined by X-ray diffraction at 1.7 Å resolution. Released 15 Aug 2012.
Explore 3SWK in 3D Show helices and sheets RCSB PDB PDBe
3SWK 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 | 155-207 | 53 | |
| α-helix | 210-234 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 154-236 | 83 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vimentin | A, B | protein | 86 | Homo sapiens | P08670 (AlphaFold model) |
>3SWK_1 Vimentin (chains A, B) EMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDN ASLARLDLERKVESLQEEIAFLKKLH
Atomic structure of the vimentin central alpha-helical domain and its implications for intermediate filament assembly. Chernyatina, A.A., Nicolet, S., Aebi, U. et al. Proc Natl Acad Sci U S A (2012) 109:13620-13625. DOI 10.1073/pnas.1206836109 · 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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