The structure of bcl-W reveals a role for the C-terminal residues in modulating biological activity. Determined by solution NMR. Released 1 Apr 2003.
Explore 1O0L in 3D Show helices and sheets RCSB PDB PDBe
1O0L contains 11 α-helices and 0 β-strands across 1 chain. 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 | 10-24 | 15 | |
| α-helix | 33-35 | 3 | |
| α-helix | 43-56 | 14 | |
| α-helix | 61-67 | 7 | |
| α-helix | 76-86 | 11 | |
| α-helix | 93-111 | 19 | |
| α-helix | 116-129 | 14 | |
| α-helix | 130-134 | 5 | |
| α-helix | 135-141 | 7 | |
| α-helix | 144-150 | 7 | |
| α-helix | 157-170 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator Bcl-W | A | protein | 188 | Homo sapiens | Q92843 (AlphaFold model) |
>1O0L_1 Apoptosis regulator Bcl-W (chains A) GPLGSMATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFET RFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEM EPLVGQVQEWMVEYLETRLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLT GAVALGAL
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. Hinds, M.G., Lackmann, M., Skea, G.L. et al. EMBO J (2003) 22:1497-1507. DOI 10.1093/emboj/cdg144 · PubMed
Other PDB entries of the same protein (UniProt Q92843 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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