Structure of Bcl-xL bound to BimLOCK. Determined by X-ray diffraction at 1.9 Å resolution. Released 28 Nov 2012.
Explore 2YQ7 in 3D Show helices and sheets RCSB PDB PDBe
2YQ7 contains 11 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 | 22 | |
| α-helix | 26-100 | 19 | |
| α-helix | 102-110 | 9 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 148-163 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2-like protein 1 | A | protein | 158 | HOMO SAPIENS | Q07817 (AlphaFold model) |
| Bcl-2-like protein 11 | B | protein | 20 | HOMO SAPIENS | O43521 (AlphaFold model) |
>2YQ7_1 BCL-2-LIKE PROTEIN 1 (chains A) GPLGSMSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQ LHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMA TYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
>2YQ7_2 BCL-2-LIKE PROTEIN 11 (chains B) XWIAQELREIGDKFNAYYAX
Stabilizing the Pro-Apoptotic Bimbh3 Helix (Bimsahb) Does not Necessarily Enhance Affinity or Biological Activity. Okamoto, T., Zobel, K., Fedorova, A. et al. ACS Chem Biol (2013) 8:297. DOI 10.1021/CB3005403 · 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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