Solution structure of the UAS domain from human FAS-associated factor 1. Determined by solution NMR. Released 4 Mar 2008.
Explore 2EC4 in 3D Show helices and sheets RCSB PDB PDBe
2EC4 contains 7 α-helices and 4 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 | 13-28 | 16 | |
| α-helix | 40-45 | 6 | |
| β-strand | 57-63 | 7 | 1 |
| α-helix | 69-76 | 8 | |
| α-helix | 81-89 | 9 | |
| β-strand | 91-97 | 7 | 1 |
| α-helix | 101-114 | 14 | |
| α-helix | 117-125 | 9 | |
| β-strand | 133-137 | 5 | 1 |
| β-strand | 146-150 | 5 | 1 |
| α-helix | 156-173 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FAS-associated factor 1 | A | protein | 178 | Homo sapiens | Q9UNN5 (AlphaFold model) |
>2EC4_1 FAS-associated factor 1 (chains A) GSSGSSGENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAI YLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRHFGSVVA QTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQQEDI
Solution structure of the UAS domain from human FAS-associated factor 1. Zhang, H.P., Hayashi, F., Yokoyama, S. To be published.
Other PDB entries of the same protein (UniProt Q9UNN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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