Crystal structure of BAXP168G monomer co-crystallized with glycerol. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Jun 2018.
Explore 5W61 in 3D Show helices and sheets RCSB PDB PDBe
5W61 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 | 16-34 | 19 | |
| α-helix | 54-71 | 18 | |
| α-helix | 74-80 | 7 | |
| α-helix | 88-100 | 13 | |
| α-helix | 107-124 | 18 | |
| α-helix | 132-143 | 12 | |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 159-166 | 8 | |
| α-helix | 170-187 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator BAX | A | protein | 194 | Homo sapiens | Q07812 (AlphaFold model) |
>5W61_1 Apoptosis regulator BAX (chains A) MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLS ESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKL VLKALSTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTGTWQTVTIFVAGV LTASLTIWKKMGSS
Ensemble Properties of Bax Determine Its Function. Robin, A.Y., Iyer, S., Birkinshaw, R.W. et al. Structure (2018) 26:1346. DOI 10.1016/j.str.2018.07.006 · 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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