Solution structure of BCL-xL in complex with PUMA BH3 peptide. Determined by solution NMR. Released 30 Jan 2013.
Explore 2M04 in 3D Show helices and sheets RCSB PDB PDBe
2M04 contains 9 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 | 3-18 | 16 | |
| α-helix | 43-94 | 12 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-177 | 41 | |
| α-helix | 179-185 | 7 | |
| α-helix | 188-196 | 9 | |
| α-helix | 199-203 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 72-83 | 12 | |
| α-helix | 84-88 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2-like protein 1 | A | protein | 180 | Homo sapiens | Q07817 (AlphaFold model) |
| Bcl-2-binding component 3 | B | protein | 25 | Homo sapiens | Q9BXH1 (AlphaFold model) |
>2M04_1 Bcl-2-like protein 1 (chains A) MSAMSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEAVKQALREAGDEF ELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDK EMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERLEHHHHHH
>2M04_2 Bcl-2-binding component 3 (chains B) EEQWAREIGAQLRRMADDLNAQYER
PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis. Follis, A.V., Chipuk, J.E., Fisher, J.C. et al. Nat Chem Biol (2013) 9:163-168. DOI 10.1038/nchembio.1166 · 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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