9RFF: Human Rac1 Fused with the Scaffold Protein POSH

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.

Method
X-ray diffraction
Resolution
1.25 Å
Organism
Homo sapiens
Chains
1
Atoms
1,958
Mol. weight
26.23 kDa
Ligands
GNP, MG
Released
3 Dec 2025

Explore 9RFF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 13 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand2-1091
α-helix16-2510
β-strand37-46101
β-strand49-58101
α-helix62-643
α-helix68-714
β-strand77-8371
α-helix87-926
α-helix93-975
α-helix98-1047
β-strand110-11561
α-helix117-1193
α-helix123-1319
α-helix136-1383
α-helix139-14810
β-strand153-15641
α-helix165-17612
β-strand32611
α-helix327-3293
β-strand330-33451
α-helix337-3448
β-strand356-36052
β-strand363-36752

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras-related C3 botulinum toxin substrate 1,E3 ubiquitin-protein ligase SH3RF1Aprotein233Homo sapiensP63000 (AlphaFold model), Q7Z6J0 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9RFF_1 Ras-related C3 botulinum toxin substrate 1,E3 ubiquitin-protein ligase SH3RF1 (chains A)
GRRMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWD
TAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKL
DLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVL
QNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPS

Ligands and cofactors

IDNameFormulaCopies
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31
MGMagnesium ionMg1

Water and common crystallization additives (MPD) are not listed.

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 9RFF directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.