Crystal Structure of Human Rac1 Fused with the Scaffold Protein POSH (residues 319-371). Determined by X-ray diffraction at 1.25 Å resolution. Released 3 Dec 2025.
Explore 9RFF in 3D Show helices and sheets RCSB PDB PDBe
9RFF contains 13 α-helices and 10 β-strands across 1 chain. 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 | 2-10 | 9 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 37-46 | 10 | 1 |
| β-strand | 49-58 | 10 | 1 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 1 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 1 |
| α-helix | 117-119 | 3 | |
| α-helix | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 153-156 | 4 | 1 |
| α-helix | 165-176 | 12 | |
| β-strand | 326 | 1 | 1 |
| α-helix | 327-329 | 3 | |
| β-strand | 330-334 | 5 | 1 |
| α-helix | 337-344 | 8 | |
| β-strand | 356-360 | 5 | 2 |
| β-strand | 363-367 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ras-related C3 botulinum toxin substrate 1,E3 ubiquitin-protein ligase SH3RF1 | A | protein | 233 | Homo sapiens | P63000 (AlphaFold model), Q7Z6J0 (AlphaFold model) |
>9RFF_1 Ras-related C3 botulinum toxin substrate 1,E3 ubiquitin-protein ligase SH3RF1 (chains A) GRRMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWD TAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKL DLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVL QNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPS
| ID | Name | Formula | Copies |
|---|---|---|---|
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (MPD) are not listed.
Hierarchical folding-upon-binding of an intrinsically disordered protein. Kjaer, L.F., Ielasi, F.S., Winbolt, T. et al. Nat Commun (2025) 16:11346-11346. DOI 10.1038/s41467-025-66420-5 · 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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