Bax domain swapped dimer in complex with BidBH3. Determined by X-ray diffraction at 2.21 Å resolution. Released 13 Feb 2013.
Explore 4BD2 in 3D Show helices and sheets RCSB PDB PDBe
4BD2 contains 10 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 | 16-36 | 21 | |
| α-helix | 54-72 | 19 | |
| α-helix | 74-82 | 9 | |
| α-helix | 88-99 | 12 | |
| α-helix | 107-143 | 37 | |
| α-helix | 144-148 | 5 | |
| α-helix | 149-154 | 6 | |
| α-helix | 159-164 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 77-96 | 20 | |
| α-helix | 97-99 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator bax | A | protein | 174 | HOMO SAPIENS | Q07812 (AlphaFold model) |
| BH3-interacting domain death agonist | C | protein | 34 | HOMO SAPIENS | P55957 (AlphaFold model) |
>4BD2_1 APOPTOSIS REGULATOR BAX (chains A) MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLS ESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKL VLKALSTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQGSS
>4BD2_2 BH3-INTERACTING DOMAIN DEATH AGONIST (chains C) SESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGL
Bax Crystal Structures Reveal How Bh3 Domains Activate Bax and Nucleate its Oligomerization to Induce Apoptosis. Czabotar, P.E., Westphal, D., Dewson, G. et al. Cell (2013) 152:519. DOI 10.1016/J.CELL.2012.12.031 · 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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