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.
Explore 5O2Z in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 161-167 | 7 | 2 |
| β-strand | 171-176 | 6 | 1 |
| α-helix | 180-182 | 3 | |
| β-strand | 188-192 | 5 | 1 |
| β-strand | 196-201 | 6 | 1 |
| α-helix | 207-219 | 13 | |
| α-helix | 220-224 | 5 | |
| β-strand | 230-235 | 6 | 1 |
| α-helix | 241-247 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gelsolin | A, B | protein | 119 | Homo sapiens | P06396 (AlphaFold model) |
>5O2Z_1 Gelsolin (chains A, B) GSHHVVPNEVVVQRLFQVKRRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNR YERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAA
Water and common crystallization additives (ACT, NA, GOL) are not listed.
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:
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