Human Bcl-2 (G101V Mutant)/Bcl-xL Chimera Fused to Maltose-Binding Protein. Determined by X-ray diffraction at 1.77 Å resolution. Released 2 Oct 2024.
Explore 8VWX in 3D Show helices and sheets RCSB PDB PDBe
8VWX contains 31 α-helices and 24 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 | -366--364 | 3 | |
| β-strand | -356--353 | 4 | 1 |
| α-helix | -346--332 | 15 | |
| β-strand | -328--325 | 4 | 1 |
| α-helix | -320--312 | 9 | |
| β-strand | -304--300 | 5 | 1 |
| α-helix | -299--297 | 3 | |
| α-helix | -296--291 | 6 | |
| β-strand | -287 | 1 | 2 |
| β-strand | -284 | 1 | 3 |
| α-helix | -280--277 | 4 | |
| β-strand | -274 | 1 | 4 |
| α-helix | -272--267 | 6 | |
| β-strand | -265--264 | 2 | 3 |
| β-strand | -261--260 | 2 | 3 |
| β-strand | -257--252 | 6 | 1 |
| β-strand | -249--245 | 5 | 5 |
| β-strand | -235 | 1 | 6 |
| α-helix | -234--232 | 3 | |
| α-helix | -231--223 | 9 | |
| β-strand | -218--216 | 3 | 5 |
| α-helix | -209--200 | 10 | |
| β-strand | -196--192 | 5 | 7 |
| β-strand | -187--181 | 7 | 7 |
| α-helix | -177--163 | 15 | |
| α-helix | -153--145 | 9 | |
| β-strand | -141--136 | 6 | 5 |
| α-helix | -134--132 | 3 | |
| α-helix | -131--126 | 6 | |
| β-strand | -121--118 | 4 | 5 |
| α-helix | -117--115 | 3 | |
| β-strand | -114--113 | 2 | 6 |
| β-strand | -110--109 | 2 | 6 |
| α-helix | -106 | 1 | |
| β-strand | -105--104 | 2 | 8 |
| β-strand | -103--97 | 7 | 1 |
| β-strand | -96 | 1 | 2 |
| α-helix | -90--84 | 7 | |
| α-helix | -83--79 | 5 | |
| α-helix | -76--67 | 10 | |
| β-strand | -62--61 | 2 | 1 |
| β-strand | -59 | 1 | 4 |
| α-helix | -58--52 | 7 | |
| α-helix | -48--38 | 11 | |
| β-strand | -35--34 | 2 | 8 |
| α-helix | -33--32 | 2 | |
| α-helix | -27--11 | 17 | |
| α-helix | -6-25 | 32 | |
| α-helix | 92-107 | 16 | |
| α-helix | 123-137 | 15 | |
| α-helix | 144-163 | 20 | |
| α-helix | 168-180 | 13 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-202 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein fused to apoptosis regulator Bcl-2/Bcl-xL chimera | A | protein | 547 | Escherichia coli (strain K12), Homo sapiens | P0AEX9 (AlphaFold model), P10415 (AlphaFold model), Q07817 (AlphaFold model) |
>8VWX_1 Maltose/maltodextrin-binding periplasmic protein fused to apoptosis regulator Bcl-2/Bcl-xL chimera (chains A) MHHHHHHHHHHENLYFQGKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDK LEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGK LIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIA ADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGET AMTINGPWAWSNIDTSAVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEN YLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYA VRTAVINAASGRQTVDEALKDAQTAARAAADNREIVMKYIHYKLSQRGYEWDAGDDVEEN RTEAPEGTESEVVHLTLRQAVDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRD GVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVE LYGPSMR
Hydrogen/Deuterium Exchange and Protein Oxidative Footprinting with Mass Spectrometry Collectively Discriminate the Binding of Small-Molecule Therapeutics to Bcl-2. Sun, Y., Houde, D., Iacob, R.E. et al. Anal Chem (2025) 97:4329-4340. DOI 10.1021/acs.analchem.4c04516 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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