Solution structure of the autoinhibited conformation of wasp. Determined by solution NMR. Released 5 Apr 2000.
Explore 1EJ5 in 3D Show helices and sheets RCSB PDB PDBe
1EJ5 contains 6 α-helices and 2 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 |
|---|---|---|---|
| β-strand | 12 | 1 | 1 |
| β-strand | 16 | 1 | 1 |
| α-helix | 24-32 | 9 | |
| α-helix | 37-40 | 4 | |
| α-helix | 43-55 | 13 | |
| α-helix | 58-68 | 11 | |
| α-helix | 81-88 | 8 | |
| α-helix | 89-92 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Wiskott-aldrich syndrome protein | A | protein | 107 | Homo sapiens | P42768 (AlphaFold model) |
>1EJ5_1 WISKOTT-ALDRICH SYNDROME PROTEIN (chains A) SGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLE AVRQEMRRQGGSGGSQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAG
Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Kim, A.S., Kakalis, L.T., Abdul-Manan, N. et al. Nature (2000) 404:151-158. DOI 10.1038/35010088 · PubMed
Other PDB entries of the same protein (UniProt P42768 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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