Crystal structure of Bax D71N core domain BH3-groove dimer. Determined by X-ray diffraction at 2.25 Å resolution. Released 27 Dec 2023.
Explore 8SVK in 3D Show helices and sheets RCSB PDB PDBe
8SVK contains 16 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 54-72 | 19 | |
| α-helix | 74-81 | 8 | |
| α-helix | 88-98 | 11 | |
| α-helix | 107-125 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 55-73 | 19 | |
| α-helix | 76-82 | 7 | |
| α-helix | 88-99 | 12 | |
| α-helix | 107-124 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 55-72 | 18 | |
| α-helix | 74-81 | 8 | |
| α-helix | 88-101 | 14 | |
| α-helix | 107-125 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 54-71 | 18 | |
| α-helix | 74-80 | 7 | |
| α-helix | 88-99 | 12 | |
| α-helix | 107-121 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator BAX | A, B, C, D | protein | 81 | Homo sapiens | Q07812 (AlphaFold model) |
>8SVK_1 Apoptosis regulator BAX (chains A, B, C, D) GPLGSDASTKKLSESLKRIGDELNSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNW GRVVALFYFASKLVLKALSTK
Sequence differences between BAX and BAK core domains manifest as differences in their interactions with lipids. Miller, M.S., Cowan, A.D., Brouwer, J.M. et al. FEBS J (2024) 291:2335-2353. DOI 10.1111/febs.17031 · PubMed
Other PDB entries of the same protein (UniProt Q07812 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8SVK 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.