Crystal Structure of FHA domain of human APLF. Determined by X-ray diffraction at 1.35 Å resolution. Released 2 May 2018.
Explore 5W7W in 3D Show helices and sheets RCSB PDB PDBe
5W7W contains 3 α-helices and 24 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 | 5-9 | 5 | 4 |
| β-strand | 16-17 | 2 | 4 |
| α-helix | 18-19 | 2 | |
| β-strand | 21-25 | 5 | 5 |
| β-strand | 28 | 1 | 6 |
| β-strand | 33 | 1 | 6 |
| β-strand | 43-48 | 6 | 5 |
| β-strand | 51-56 | 6 | 5 |
| β-strand | 63-65 | 3 | 4 |
| β-strand | 73-74 | 2 | 4 |
| α-helix | 75-76 | 2 | |
| β-strand | 81-83 | 3 | 5 |
| β-strand | 88-90 | 3 | 4 |
| β-strand | 97-102 | 6 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 1 |
| β-strand | 16-18 | 3 | 1 |
| β-strand | 21-25 | 5 | 2 |
| β-strand | 28 | 1 | 3 |
| β-strand | 33 | 1 | 3 |
| β-strand | 43-48 | 6 | 2 |
| β-strand | 51-56 | 6 | 2 |
| β-strand | 63-65 | 3 | 1 |
| β-strand | 73-74 | 2 | 1 |
| α-helix | 75-76 | 2 | |
| β-strand | 81-82 | 2 | 2 |
| β-strand | 88-92 | 5 | 1 |
| β-strand | 95-102 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Aprataxin and PNK-like factor | A, T | protein | 108 | Homo sapiens | Q8IW19 (AlphaFold model) |
>5W7W_1 Aprataxin and PNK-like factor (chains A, T) SFTMSGGFELQPRDGGPRVALAPGETVIGRGPLLGITDKRVSRRHAILEVAGGQLRIKPI HTNPCFYQSSEKSQLLPLKPNLWCYLNPGDSFSLLVDKYIFRILSIPS
Characterization of the APLF FHA-XRCC1 phosphopeptide interaction and its structural and functional implications. Kim, K., Pedersen, L.C., Kirby, T.W. et al. Nucleic Acids Res (2017) 45:12374-12387. DOI 10.1093/nar/gkx941 · PubMed
Other PDB entries of the same protein (UniProt Q8IW19 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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