Crystal Structure of the HHD2 Domain of Whirlin : 3-helix conformation. Determined by X-ray diffraction at 1.85 Å resolution. Released 8 Aug 2018.
Explore 6FDE in 3D Show helices and sheets RCSB PDB PDBe
6FDE contains 5 α-helices and 0 β-strands across 1 chain. 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 | 432-451 | 20 | |
| α-helix | 457-478 | 22 | |
| α-helix | 480-483 | 4 | |
| α-helix | 486-488 | 3 | |
| α-helix | 489-497 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Whirlin | A | protein | 85 | Mus musculus | Q80VW5 (AlphaFold model) |
>6FDE_1 Whirlin (chains A) GAMGSGNQTRALLDDQARHLLTEQERATMMYYLAQYRGGTISVEAMVMALFELLNTHAKF SLLSEVRSIISPQDLDRFDHLVLRR
Structural plasticity of the HHD2 domain of whirlin. Delhommel, F., Cordier, F., Saul, F. et al. FEBS J (2018) 285:3738-3752. DOI 10.1111/febs.14614 · PubMed
Other PDB entries of the same protein (UniProt Q80VW5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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