Structure of BFL1 in complex with a covalent inhibitor, alternative series, cmpd25. Determined by X-ray diffraction at 1.43 Å resolution. Released 14 Jan 2026.
Explore 9S6M in 3D Show helices and sheets RCSB PDB PDBe
9S6M contains 24 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 | 6-20 | 15 | |
| α-helix | 24-25 | 2 | |
| α-helix | 32-51 | 20 | |
| α-helix | 53-56 | 4 | |
| α-helix | 64-78 | 15 | |
| α-helix | 86-106 | 21 | |
| α-helix | 114-125 | 12 | |
| α-helix | 126-130 | 5 | |
| α-helix | 131-136 | 6 | |
| α-helix | 139 | 1 | |
| α-helix | 140-144 | 5 | |
| α-helix | 145-148 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-20 | 15 | |
| α-helix | 32-51 | 20 | |
| α-helix | 53-56 | 4 | |
| α-helix | 64-78 | 15 | |
| α-helix | 86-106 | 21 | |
| α-helix | 112-114 | 3 | |
| α-helix | 115-125 | 11 | |
| α-helix | 126-130 | 5 | |
| α-helix | 131-136 | 6 | |
| α-helix | 139 | 1 | |
| α-helix | 140-144 | 5 | |
| α-helix | 145-148 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2-related protein A1 | A, B | protein | 152 | Homo sapiens | Q16548 (AlphaFold model) |
>9S6M_1 Bcl-2-related protein A1 (chains A, B) GMTDCEFGYIYRLAQDYLQCVLQIPQPGSGPSKTSRVLQNVAFSVQKEVEKNLKSCLDNV NVVSVDTARTLFNQVMEKEFEDGIINWGRIVTIFAFEGILIKKLLRQQIAPDVDTYKEIS YFVAEFIMNNTGEWIRQNGGWENGFVKKFEPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1JL2 | (1~{R},2~{R})-2-azanyl-~{N}-[4-[(1~{R})-1-[propanoyl-[4-(trifluoromethyloxy)phe… | C24 H28 F3 N3 O3 | 2 |
Optimization and Chemoproteomic Profiling of a Selective, Covalent Bfl-1-Targeting Cellular Tool. Blackwell, J.H., Lucas, S.C.C., Battocchio, G. et al. J Med Chem (2026) 69:1218-1246. DOI 10.1021/acs.jmedchem.5c02581 · PubMed
Other PDB entries of the same protein (UniProt Q16548 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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