Bcl-xL with Bak BH3 complex. Determined by X-ray diffraction at 1.73 Å resolution. Released 1 Jun 2016.
Explore 5FMK in 3D Show helices and sheets RCSB PDB PDBe
5FMK contains 12 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 | 59-75 | 17 | |
| α-helix | 82-105 | 24 | |
| α-helix | 108-111 | 4 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 161-173 | 13 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 | |
| α-helix | 199-206 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 70-85 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-xl | A | protein | 158 | HOMO SAPIENS | Q07817 (AlphaFold model) |
| Bcl-2 homologous antagonist/killer | B | protein | 34 | HOMO SAPIENS | Q16611 (AlphaFold model) |
>5FMK_1 BCL-XL (chains A) GPLGSMSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQ LHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMA TYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
>5FMK_2 BCL-2 HOMOLOGOUS ANTAGONIST/KILLER (chains B) LPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTM
Physiological Restraint of Bak by Bcl-Xl is Essential for Cell Survival. Lee, E.F., Grabow, S., Chappaz, S. et al. Genes Dev (2016) 30:1240. DOI 10.1101/GAD.279414.116 · PubMed
Other PDB entries of the same protein (UniProt Q07817 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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