Bak L100A. Determined by X-ray diffraction at 1.22 Å resolution. Released 15 Nov 2017.
Explore 5VX1 in 3D Show helices and sheets RCSB PDB PDBe
5VX1 contains 20 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 | 24-47 | 24 | |
| α-helix | 63-64 | 2 | |
| α-helix | 70-80 | 11 | |
| α-helix | 84-100 | 17 | |
| α-helix | 107-119 | 13 | |
| α-helix | 125-145 | 21 | |
| α-helix | 151-164 | 14 | |
| α-helix | 167-173 | 7 | |
| α-helix | 177-181 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-50 | 27 | |
| α-helix | 55-57 | 3 | |
| α-helix | 58-61 | 4 | |
| α-helix | 63-64 | 2 | |
| α-helix | 70-79 | 10 | |
| α-helix | 84-100 | 17 | |
| α-helix | 107-119 | 13 | |
| α-helix | 125-144 | 20 | |
| α-helix | 151-164 | 14 | |
| α-helix | 167-173 | 7 | |
| α-helix | 177-181 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2 homologous antagonist/killer | A, B | protein | 170 | Homo sapiens | Q16611 (AlphaFold model) |
>5VX1_1 Bcl-2 homologous antagonist/killer (chains A, B) GPLGSMSEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGR QLAIIGDDINRRYDSEFQTMLQHAQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGY RLALHVYQHGLTGFLGQVTRFVVDFMLHHSIARWIAQRGGWVAALNLGNG
Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design. Brouwer, J.M., Lan, P., Cowan, A.D. et al. Mol Cell (2017) 68:659-672.e9. DOI 10.1016/j.molcel.2017.11.001 · PubMed
Other PDB entries of the same protein (UniProt Q16611 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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