Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase. Determined by X-ray diffraction at 1.75 Å resolution. Released 27 Jan 2004.
Explore 1RYF in 3D Show helices and sheets RCSB PDB PDBe
1RYF contains 18 α-helices and 12 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 | 2A-10 | 11 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 39-46 | 8 | 1 |
| β-strand | 49-57 | 9 | 1 |
| β-strand | 96-102 | 7 | 1 |
| α-helix | 106-111 | 6 | |
| α-helix | 112-116 | 5 | |
| α-helix | 117-123 | 7 | |
| β-strand | 129-134 | 6 | 1 |
| α-helix | 136-139 | 4 | |
| α-helix | 142-149 | 8 | |
| α-helix | 155-157 | 3 | |
| α-helix | 158-168 | 11 | |
| β-strand | 172-175 | 4 | 1 |
| α-helix | 184-196 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2A-10 | 11 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 39-46 | 8 | 1 |
| β-strand | 49-57 | 9 | 1 |
| β-strand | 96-102 | 7 | 1 |
| α-helix | 106-111 | 6 | |
| α-helix | 112-116 | 5 | |
| α-helix | 117-123 | 7 | |
| β-strand | 129-134 | 6 | 1 |
| α-helix | 136-139 | 4 | |
| α-helix | 142-150 | 9 | |
| α-helix | 155-157 | 3 | |
| α-helix | 158-168 | 11 | |
| β-strand | 172-175 | 4 | 1 |
| α-helix | 184-196 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ras-related C3 botulinum toxin substrate 1 isoform Rac1b | A, B | protein | 203 | Homo sapiens | P63000 (AlphaFold model) |
>1RYF_1 ras-related C3 botulinum toxin substrate 1 isoform Rac1b (chains A, B) GSMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDT AGQEDYDRLRPLSYPQTVGETYGKDITSRGKDKPIADVFLICFSLVSPASFENVRAKWYP EVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSA LTQRGLKTVFDEAIRAVLCPPPV
Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase. Fiegen, D., Haeusler, L.C., Blumenstein, L. et al. J Biol Chem (2004) 279:4743-4749. DOI 10.1074/jbc.M310281200 · PubMed
Other PDB entries of the same protein (UniProt P63000 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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