Crystal structure of human SOUL protein (hexagonal form). Determined by X-ray diffraction at 2.85 Å resolution. Released 29 Jun 2011.
Explore 3R8K in 3D Show helices and sheets RCSB PDB PDBe
3R8K contains 29 α-helices and 58 β-strands across 4 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 | 25-26 | 2 | 1 |
| α-helix | 29-31 | 3 | |
| α-helix | 34 | 1 | |
| β-strand | 39-43 | 5 | 2 |
| α-helix | 44-45 | 2 | |
| β-strand | 46-55 | 10 | 2 |
| α-helix | 58-73 | 16 | |
| β-strand | 77 | 1 | 3 |
| α-helix | 88 | 1 | |
| β-strand | 89-94 | 6 | 2 |
| β-strand | 103-110 | 8 | 2 |
| α-helix | 119-121 | 3 | |
| β-strand | 122 | 1 | 3 |
| β-strand | 127-132 | 6 | 2 |
| α-helix | 133-134 | 2 | |
| β-strand | 135-141 | 7 | 2 |
| α-helix | 148-164 | 17 | |
| β-strand | 169 | 1 | 4 |
| β-strand | 174-178 | 5 | 2 |
| β-strand | 191-195 | 5 | 2 |
| β-strand | 196 | 1 | 4 |
| α-helix | 197 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 25-26 | 2 | 2 |
| α-helix | 29-31 | 3 | |
| α-helix | 33-34 | 2 | |
| β-strand | 39-43 | 5 | 1 |
| α-helix | 44-45 | 2 | |
| β-strand | 46-53 | 8 | 1 |
| α-helix | 58-74 | 17 | |
| β-strand | 77 | 1 | 5 |
| β-strand | 89-94 | 6 | 1 |
| β-strand | 104-110 | 7 | 1 |
| β-strand | 122 | 1 | 5 |
| β-strand | 127-132 | 6 | 1 |
| α-helix | 133-134 | 2 | |
| β-strand | 135-141 | 7 | 1 |
| α-helix | 148-164 | 17 | |
| β-strand | 169 | 1 | 6 |
| β-strand | 174-178 | 5 | 1 |
| β-strand | 191-195 | 5 | 1 |
| β-strand | 196 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 21 | 1 | 7 |
| β-strand | 25-26 | 2 | 8 |
| β-strand | 39-43 | 5 | 8 |
| β-strand | 46-55 | 10 | 8 |
| α-helix | 58-74 | 17 | |
| β-strand | 77 | 1 | 9 |
| β-strand | 86 | 1 | 7 |
| α-helix | 88 | 1 | |
| β-strand | 89 | 1 | 10 |
| β-strand | 90-94 | 5 | 8 |
| β-strand | 103-110 | 8 | 8 |
| α-helix | 113-116 | 4 | |
| α-helix | 119-121 | 3 | |
| β-strand | 122 | 1 | 9 |
| β-strand | 127-132 | 6 | 8 |
| α-helix | 133-134 | 2 | |
| β-strand | 135-141 | 7 | 8 |
| α-helix | 148-163 | 16 | |
| β-strand | 169 | 1 | 11 |
| β-strand | 174-177 | 4 | 8 |
| β-strand | 178 | 1 | 10 |
| β-strand | 191-195 | 5 | 8 |
| β-strand | 196 | 1 | 11 |
| α-helix | 197 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 21 | 1 | 12 |
| β-strand | 25-26 | 2 | 13 |
| β-strand | 39-43 | 5 | 13 |
| α-helix | 44-45 | 2 | |
| β-strand | 46-55 | 10 | 13 |
| α-helix | 58-74 | 17 | |
| β-strand | 77 | 1 | 14 |
| β-strand | 86 | 1 | 12 |
| β-strand | 89-94 | 6 | 13 |
| β-strand | 103-110 | 8 | 13 |
| α-helix | 113-115 | 3 | |
| α-helix | 119-121 | 3 | |
| β-strand | 122 | 1 | 14 |
| β-strand | 127-132 | 6 | 13 |
| α-helix | 133-134 | 2 | |
| β-strand | 135-141 | 7 | 13 |
| α-helix | 148-164 | 17 | |
| β-strand | 169 | 1 | 15 |
| β-strand | 174-178 | 5 | 13 |
| β-strand | 191-195 | 5 | 13 |
| β-strand | 196 | 1 | 15 |
| α-helix | 197 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heme-binding protein 2 | A, B, C, D | protein | 212 | Homo sapiens | Q9Y5Z4 (AlphaFold model) |
>3R8K_1 Heme-binding protein 2 (chains A, B, C, D) MRGSAEPLQPDPGAAEDAAAQAVETPGWKAPEDAGPQPGSYEIRHYGPAKWVSTSVESMD WDSAIQTGFTKLNSYIQGKNEKEMKIKMTAPVTSYVEPGSGPFSESTITISLYIPSEQQF DPPRPLESDVFIEDRAEMTVFVRSFDGFSSAQKNQEQLLTLASILREDGKVFDEKVYYTA GYNSPVKLLNRNNEVWLIQKNEPTKENELVPR
Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL. Ambrosi, E., Capaldi, S., Bovi, M. et al. Biochem J (2011) 438:291-301. DOI 10.1042/BJ20110257 · PubMed
Other PDB entries of the same protein (UniProt Q9Y5Z4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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