The NMR structure of the BID-BAK complex. Determined by solution NMR. Released 17 Apr 2013.
Explore 2M5B in 3D Show helices and sheets RCSB PDB PDBe
2M5B contains 10 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 | 24-49 | 26 | |
| α-helix | 70-81 | 12 | |
| α-helix | 83-97 | 15 | |
| α-helix | 107-118 | 12 | |
| α-helix | 125-145 | 21 | |
| α-helix | 151-162 | 12 | |
| α-helix | 167-173 | 7 | |
| α-helix | 177-182 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 81-88 | 8 | |
| α-helix | 95-99 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2 homologous antagonist/killer | A | protein | 169 | Homo sapiens | Q16611 (AlphaFold model) |
| human_BID_BH3_SAHB | B | protein | 23 | Synthetic construct | P55957 (AlphaFold model) |
>2M5B_1 Bcl-2 homologous antagonist/killer (chains A) ALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQ LAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYR LALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNG
>2M5B_2 human_BID_BH3_SAHB (chains B) EDIIRNIARHLALVGDLLDRSIX
BID-induced structural changes in BAK promote apoptosis. Moldoveanu, T., Grace, C.R., Llambi, F. et al. Nat Struct Mol Biol (2013) 20:589-597. DOI 10.1038/nsmb.2563 · PubMed
Other PDB entries of the same protein (UniProt Q16611 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2M5B directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.