5FAE: N184K pathological variant of gelsolin domain 2

N184K pathological variant of gelsolin domain 2 (trigonal form). Determined by X-ray diffraction at 1.7 Å resolution. Released 5 Oct 2016.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
1
Atoms
988
Mol. weight
13.75 kDa
Ligands
CA
Released
5 Oct 2016

Explore 5FAE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5FAE contains 5 α-helices and 5 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: 5 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand161-16661
β-strand172-17651
α-helix180-1823
β-strand188-19251
β-strand196-20161
α-helix207-21913
α-helix220-2245
β-strand230-23561
α-helix241-2477
α-helix250-2545

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GelsolinAprotein119Homo sapiensP06396 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5FAE_1 Gelsolin (chains A)
GSHHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFKNGDCFILDLGNNIHQWCGSNSNR
YERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAA

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1

Water and common crystallization additives (CL, PEG, SO4) are not listed.

Primary citation

Molecular basis of a novel renal amyloidosis due to N184K gelsolin variant. Boni, F., Milani, M., Porcari, R. et al. Sci Rep (2016) 6:33463-33463. DOI 10.1038/srep33463 · PubMed

Other PDB entries of the same protein (UniProt P06396 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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