5O2Z: Gelsolin

Domain swap dimer of the G167R variant of gelsolin second domain. Determined by X-ray diffraction at 1.7 Å resolution. Released 8 Nov 2017.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
2
Atoms
2,079
Mol. weight
27.25 kDa
Ligands
CA, FLC
Released
8 Nov 2017

Explore 5O2Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5O2Z contains 8 α-helices and 10 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.

Chains A and B: 4 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand161-16772
β-strand171-17661
α-helix180-1823
β-strand188-19251
β-strand196-20161
α-helix207-21913
α-helix220-2245
β-strand230-23561
α-helix241-2477

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GelsolinA, Bprotein119Homo sapiensP06396 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5O2Z_1 Gelsolin (chains A, B)
GSHHVVPNEVVVQRLFQVKRRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNR
YERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAA

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
FLCCitrate anionC6 H5 O72

Water and common crystallization additives (ACT, NA, GOL) are not listed.

Primary citation

Gelsolin pathogenic Gly167Arg mutation promotes domain-swap dimerization of the protein. Boni, F., Milani, M., Barbiroli, A. et al. Hum Mol Genet (2018) 27:53-65. DOI 10.1093/hmg/ddx383 · PubMed

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

Browse structure collections

About this viewer

MolViewer shows 5O2Z 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.