Crystal structure of truncated human rhogdi quadruple mutant. Determined by X-ray diffraction at 2.0 Å resolution. Released 2 May 2001.
Explore 1FSO in 3D Show helices and sheets RCSB PDB PDBe
1FSO contains 3 α-helices and 11 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 | 70-78 | 9 | 1 |
| β-strand | 87-89 | 3 | 1 |
| α-helix | 94-99 | 6 | |
| β-strand | 102-105 | 4 | 2 |
| β-strand | 109-110 | 2 | 3 |
| β-strand | 111-118 | 8 | 1 |
| β-strand | 123-134 | 12 | 2 |
| β-strand | 137-149 | 13 | 2 |
| β-strand | 152-159 | 8 | 1 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-164 | 2 | 3 |
| α-helix | 169-171 | 3 | |
| β-strand | 173-182 | 10 | 2 |
| β-strand | 188-199 | 12 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho GDP-dissociation inhibitor 1 | A | protein | 139 | Homo sapiens | P52565 (AlphaFold model) |
>1FSO_1 RHO GDP-DISSOCIATION INHIBITOR 1 (chains A) MVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSG MKYIQHTYRAGVAIDATDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDDD KTDHLSWEWNFTIKKDWKD
Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI. Longenecker, K.L., Garrard, S.M., Sheffield, P.J. et al. Acta Crystallogr D Biol Crystallogr (2001) 57:679-688. DOI 10.1107/S0907444901003122 · PubMed
Other PDB entries of the same protein (UniProt P52565 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1FSO 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.