Crystal Structure of the Autoinhibited Dimer of Pro-apoptotic BAX (I). Determined by X-ray diffraction at 1.9 Å resolution. Released 20 Jul 2016.
Explore 4S0O in 3D Show helices and sheets RCSB PDB PDBe
4S0O contains 25 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 16-34 | 19 | |
| α-helix | 43-45 | 3 | |
| α-helix | 46-51 | 6 | |
| α-helix | 54-71 | 18 | |
| α-helix | 74-81 | 8 | |
| α-helix | 89-99 | 11 | |
| α-helix | 107-126 | 20 | |
| α-helix | 131-143 | 13 | |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-164 | 7 | |
| α-helix | 170-191 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-34 | 19 | |
| α-helix | 43-45 | 3 | |
| α-helix | 46-51 | 6 | |
| α-helix | 54-71 | 18 | |
| α-helix | 74-81 | 8 | |
| α-helix | 89-99 | 11 | |
| α-helix | 107-126 | 20 | |
| α-helix | 131-143 | 13 | |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 158-160 | 3 | |
| α-helix | 161-164 | 4 | |
| α-helix | 170-191 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator BAX | A, B | protein | 192 | Homo sapiens | Q07812 (AlphaFold model) |
>4S0O_1 Apoptosis regulator BAX (chains A, B) MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLS ECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKL VLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTGTWQTVTIFVAGV LTASLTIWKKMG
An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway. Garner, T.P., Reyna, D.E., Priyadarshi, A. et al. Mol Cell (2016) 63:485-497. DOI 10.1016/j.molcel.2016.06.010 · PubMed
Other PDB entries of the same protein (UniProt Q07812 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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