1FSO: Truncated human rhogdi quadruple mutant

Crystal structure of truncated human rhogdi quadruple mutant. Determined by X-ray diffraction at 2.0 Å resolution. Released 2 May 2001.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,304
Mol. weight
15.83 kDa
Released
2 May 2001

Explore 1FSO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 3 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand70-7891
β-strand87-8931
α-helix94-996
β-strand102-10542
β-strand109-11023
β-strand111-11881
β-strand123-134122
β-strand137-149132
β-strand152-15981
α-helix160-1623
β-strand163-16423
α-helix169-1713
β-strand173-182102
β-strand188-199122

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rho GDP-dissociation inhibitor 1Aprotein139Homo sapiensP52565 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1FSO_1 RHO GDP-DISSOCIATION INHIBITOR 1 (chains A)
MVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSG
MKYIQHTYRAGVAIDATDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDDD
KTDHLSWEWNFTIKKDWKD

Primary citation

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:

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