Human WASP/WIP complex. Determined by solution NMR. Released 19 Aug 2026.
Explore 9S9X in 3D Show helices and sheets RCSB PDB PDBe
9S9X contains 4 α-helices and 8 β-strands across 2 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 | 29-38 | 10 | |
| β-strand | 44-56 | 13 | 1 |
| β-strand | 64-76 | 13 | 1 |
| β-strand | 84-88 | 5 | 1 |
| β-strand | 97 | 1 | 1 |
| β-strand | 100 | 1 | 1 |
| β-strand | 114-118 | 5 | 1 |
| β-strand | 123-128 | 6 | 1 |
| α-helix | 131-149 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 445 | 1 | 2 |
| α-helix | 447-452 | 6 | |
| α-helix | 476-481 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin nucleation-promoting factor WAS | A | protein | 141 | Homo sapiens | P42768 (AlphaFold model) |
| WAS/WASL-interacting protein family member 1 | B | protein | 53 | Homo sapiens | O43516 (AlphaFold model) |
>9S9X_1 Actin nucleation-promoting factor WAS (chains A) SGQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKD NPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAF RALVQEKIQKRNQRQSGDRRQ
>9S9X_2 WAS/WASL-interacting protein family member 1 (chains B) SGQDSPCEDEWESRFYFHPISDLPPPEPYVQTTKSYPSKLARNESRSGSNRRE
Structure of the human WASP-EVH1/WIP complex: Molecular basis of the WIP chaperone function. Sasson, I., Baluom, S., Halle-Bikovski, A. et al. To be published.
Other PDB entries of the same protein (UniProt P42768 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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