Crystal structure of BAX W139A monomer. Determined by X-ray diffraction at 2.02 Å resolution. Released 10 Apr 2019.
Explore 6EB6 in 3D Show helices and sheets RCSB PDB PDBe
6EB6 contains 10 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-39 | 24 | |
| α-helix | 54-71 | 18 | |
| α-helix | 74-81 | 8 | |
| α-helix | 88-99 | 12 | |
| α-helix | 107-126 | 20 | |
| α-helix | 131-143 | 13 | |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 159-165 | 7 | |
| α-helix | 170-189 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator BAX | A | protein | 192 | Homo sapiens | Q07812 (AlphaFold model) |
>6EB6_1 Apoptosis regulator BAX (chains A) MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLS ECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKL VLKALCTKVPELIRTIMGATLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGV LTASLTIWKKMG
BAX Activation: Mutations Near Its Proposed Non-canonical BH3 Binding Site Reveal Allosteric Changes Controlling Mitochondrial Association. Dengler, M.A., Robin, A.Y., Gibson, L. et al. Cell Rep (2019) 27:359-373.e6. DOI 10.1016/j.celrep.2019.03.040 · PubMed
Other PDB entries of the same protein (UniProt Q07812 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6EB6 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.