3S5F: Human frataxin variant W155F

Crystal structure of human frataxin variant W155F. Determined by X-ray diffraction at 1.5 Å resolution. Released 29 Jun 2011.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
2
Atoms
2,087
Mol. weight
28.36 kDa
Ligands
MG
Released
29 Jun 2011

Explore 3S5F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3S5F contains 7 α-helices and 14 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.

Chain A: 2 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix92-11322
β-strand124-12851
β-strand131-13551
β-strand142-14871
β-strand153-15861
β-strand162-16871
β-strand173-17531
β-strand18111
α-helix182-19413
Chain B: 5 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix87-893
α-helix92-11221
α-helix113-1153
β-strand124-12852
β-strand131-13552
β-strand142-14872
α-helix149-1513
β-strand153-15862
β-strand162-16872
β-strand173-17422
β-strand18112
α-helix182-19413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Frataxin, mitochondrialA, Bprotein129Homo sapiensQ16595 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3S5F_1 Frataxin, mitochondrial (chains A, B)
GTLGHPGSLDETTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLG
TYVINKQTPNKQIFLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLS
SLAYSGKDA

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2

Primary citation

Friedreich's Ataxia Variants I154F and W155R Diminish Frataxin-Based Activation of the Iron-Sulfur Cluster Assembly Complex. Tsai, C.L., Bridwell-Rabb, J., Barondeau, D.P. Biochemistry (2011) 50:6478-6487. DOI 10.1021/bi200666h · PubMed

Other PDB entries of the same protein (UniProt Q16595 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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