Solution structure of the third spectrin repeat of alpha-actinin-4. Determined by solution NMR. Released 9 Aug 2005.
Explore 1WLX in 3D Show helices and sheets RCSB PDB PDBe
1WLX contains 4 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 | 3-36 | 34 | |
| α-helix | 38-39 | 2 | |
| α-helix | 44-84 | 41 | |
| α-helix | 100-125 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-actinin 4 | A | protein | 129 | Homo sapiens | O43707 (AlphaFold model) |
>1WLX_1 Alpha-actinin 4 (chains A) GSTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKST LPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHA LLEEQSKQQ
Solution structure of the third spectrin repeat of alpha-actinin-4. Kowalski, K., Merkel, A.L., Booker, G.W. To be published.
Other PDB entries of the same protein (UniProt O43707 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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