The structure of the AXH domain of ataxin-1. Determined by X-ray diffraction at 2.5 Å resolution. Released 27 Mar 2013.
Explore 4APT in 3D Show helices and sheets RCSB PDB PDBe
4APT contains 19 α-helices and 38 β-strands across 4 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 | 566 | 1 | 1 |
| α-helix | 573-575 | 3 | |
| β-strand | 580-582 | 3 | 2 |
| β-strand | 588-590 | 3 | 2 |
| α-helix | 591-593 | 3 | |
| α-helix | 596-605 | 10 | |
| β-strand | 609-621 | 13 | 1 |
| β-strand | 627-634 | 8 | 1 |
| β-strand | 639-646 | 8 | 1 |
| β-strand | 651-653 | 3 | 1 |
| β-strand | 657-660 | 4 | 1 |
| α-helix | 663-669 | 7 | |
| β-strand | 675-676 | 2 | 1 |
| α-helix | 677 | 1 | |
| β-strand | 682-688 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 574-576 | 3 | |
| β-strand | 580-582 | 3 | 2 |
| β-strand | 588-590 | 3 | 2 |
| α-helix | 591-593 | 3 | |
| α-helix | 596-600 | 5 | |
| β-strand | 609-621 | 13 | 3 |
| β-strand | 627-634 | 8 | 3 |
| β-strand | 639-646 | 8 | 3 |
| β-strand | 651-653 | 3 | 3 |
| β-strand | 657-660 | 4 | 3 |
| α-helix | 663-670 | 8 | |
| β-strand | 675-676 | 2 | 3 |
| β-strand | 682-688 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 566 | 1 | 4 |
| α-helix | 573-575 | 3 | |
| β-strand | 580-582 | 3 | 5 |
| β-strand | 588-590 | 3 | 5 |
| α-helix | 591-593 | 3 | |
| α-helix | 596-605 | 10 | |
| β-strand | 609-621 | 13 | 4 |
| β-strand | 627-633 | 7 | 4 |
| β-strand | 640-646 | 7 | 4 |
| β-strand | 651-653 | 3 | 4 |
| β-strand | 657-660 | 4 | 4 |
| α-helix | 663-670 | 8 | |
| β-strand | 675-676 | 2 | 4 |
| α-helix | 677 | 1 | |
| β-strand | 682-688 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 568-570 | 3 | |
| α-helix | 574-576 | 3 | |
| β-strand | 580-582 | 3 | 5 |
| β-strand | 588-590 | 3 | 5 |
| α-helix | 591-593 | 3 | |
| α-helix | 596-605 | 10 | |
| β-strand | 610-621 | 12 | 4 |
| β-strand | 627-634 | 8 | 4 |
| β-strand | 640-646 | 7 | 4 |
| β-strand | 651-653 | 3 | 4 |
| β-strand | 657-660 | 4 | 4 |
| α-helix | 663-670 | 8 | |
| β-strand | 675-676 | 2 | 4 |
| β-strand | 682-687 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ataxin-1 | A, B, C, D | protein | 126 | HOMO SAPIENS | P54253 (AlphaFold model) |
>4APT_1 ATAXIN-1 (chains A, B, C, D) GAMAPPTLPPYFMKGSIIQLANGELKKVEDLKTEDFIQSAEISNDLKIDSSTVERIEDSH SPGVAVIQFAVGEHRAQVSVEVLVEYPFFVFGQGWSSCCPERTSQLFDLPCSKLSVGDVC ISLTLK
Self-Assembly and Conformational Heterogeneity of the Axh Domain of Ataxin-1: An Unusual Example of a Chameleon Fold. De Chiara, C., Rees, M., Menon, R.P. et al. Biophys J (2013) 104:1304. DOI 10.1016/J.BPJ.2013.01.048 · PubMed
Other PDB entries of the same protein (UniProt P54253 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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