Trimeric crystal structure of vimentin coil1B fragment. Determined by X-ray diffraction at 2.0 Å resolution. Released 2 Dec 2015.
Explore 4YV3 in 3D Show helices and sheets RCSB PDB PDBe
4YV3 contains 3 α-helices and 0 β-strands across 3 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 | 163-237 | 75 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 165-236 | 72 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 179-236 | 58 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vimentin | A, B, C | protein | 78 | Homo sapiens | P08670 (AlphaFold model) |
>4YV3_1 Vimentin (chains A, B, C) VDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDL ERKVESLQEEIAFLKKLH
How to Study Intermediate Filaments in Atomic Detail. Chernyatina, A.A., Hess, J.F., Guzenko, D. et al. Methods Enzymol (2016) 568:3-33. DOI 10.1016/bs.mie.2015.09.024 · 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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