Solution Structure of the GTPase Binding Domain of WASP in Complex with EspFU, an EHEC Effector. Determined by solution NMR. Released 22 Jul 2008.
Explore 2K42 in 3D Show helices and sheets RCSB PDB PDBe
2K42 contains 6 α-helices and 2 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 |
|---|---|---|---|
| β-strand | 14-15 | 2 | 1 |
| β-strand | 19-20 | 2 | 1 |
| α-helix | 27-36 | 10 | |
| α-helix | 40-43 | 4 | |
| α-helix | 46-58 | 13 | |
| α-helix | 62-69 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 79-88 | 10 | |
| α-helix | 92-94 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Wiskott-Aldrich syndrome protein | A | protein | 72 | Homo sapiens | P42768 (AlphaFold model) |
| Espfu | B | protein | 36 | Escherichia coli O157:H7 | Q8X482 |
>2K42_1 Wiskott-Aldrich syndrome protein (chains A) GHMSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQG GLEAVRQEMRRQ
>2K42_2 ESPFU (chains B) GHMLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNW
Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U). Cheng, H.C., Skehan, B.M., Campellone, K.G. et al. Nature (2008) 454:1009-1013. DOI 10.1038/nature07160 · 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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