Bim BH3 peptide in complex with Bcl-xL. Determined by X-ray diffraction at 1.78 Å resolution. Released 10 Mar 2009.
Explore 3FDL in 3D Show helices and sheets RCSB PDB PDBe
3FDL 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 | -4-19 | 23 | |
| α-helix | 26-100 | 19 | |
| α-helix | 102-110 | 9 | |
| 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 | 187-193 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 87-105 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator Bcl-X | A | protein | 158 | Homo sapiens | Q07817 (AlphaFold model) |
| Bcl-2-like protein 11 | B | protein | 26 | synthetic construct | O43521 (AlphaFold model) |
>3FDL_1 Apoptosis regulator Bcl-X (chains A) GPLGSMSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQ LHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMA TYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
>3FDL_2 Bcl-2-like protein 11 (chains B) DMRPEIWIAQELRRIGDEFNAYYARR
High-Resolution Structural Characterization of a Helical alpha/beta-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-x(L). Lee, E.F., Sadowsky, J.D., Smith, B.J. et al. Angew Chem Int Ed Engl (2009) 48:4318-4322. DOI 10.1002/anie.200805761 · 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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