Structural basis for mutation-induced destabilization of Profilin 1 in ALS. Determined by X-ray diffraction at 2.23 Å resolution. Released 10 Jun 2015.
Explore 4X25 in 3D Show helices and sheets RCSB PDB PDBe
4X25 contains 10 α-helices and 17 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 | 5-11 | 7 | |
| β-strand | 17-24 | 8 | 1 |
| β-strand | 30-34 | 5 | 1 |
| α-helix | 40-42 | 3 | |
| α-helix | 45-51 | 7 | |
| β-strand | 55 | 1 | 2 |
| α-helix | 58-61 | 4 | |
| β-strand | 64-66 | 3 | 1 |
| β-strand | 69-77 | 9 | 1 |
| β-strand | 85-90 | 6 | 1 |
| β-strand | 100-105 | 6 | 1 |
| β-strand | 109-115 | 7 | 1 |
| α-helix | 121-137 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-11 | 7 | |
| β-strand | 17-24 | 8 | 3 |
| β-strand | 30-34 | 5 | 3 |
| α-helix | 40-42 | 3 | |
| α-helix | 45-51 | 7 | |
| β-strand | 55 | 1 | 2 |
| α-helix | 58-62 | 5 | |
| β-strand | 64-66 | 3 | 4 |
| β-strand | 69-71 | 3 | 4 |
| β-strand | 72-76 | 5 | 3 |
| β-strand | 85-89 | 5 | 3 |
| β-strand | 100-105 | 6 | 3 |
| β-strand | 109-115 | 7 | 3 |
| α-helix | 121-137 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Profilin-1 | A, B | protein | 140 | Homo sapiens | P07737 (AlphaFold model) |
>4X25_1 Profilin-1 (chains A, B) MAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFY VNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLTGKEGVH GGLINKKCYEMASHLRRSQY
Structural basis for mutation-induced destabilization of profilin 1 in ALS. Boopathy, S., Silvas, T.V., Tischbein, M. et al. Proc Natl Acad Sci U S A (2015) 112:7984-7989. DOI 10.1073/pnas.1424108112 · PubMed
Other PDB entries of the same protein (UniProt P07737 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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