Crystal Structure of human BAK in complex with W3W5_BID. Determined by X-ray diffraction at 1.5 Å resolution. Released 12 Jan 2022.
Explore 7M5A in 3D Show helices and sheets RCSB PDB PDBe
7M5A 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 | 23-48 | 26 | |
| α-helix | 58-60 | 3 | |
| α-helix | 71-81 | 11 | |
| α-helix | 83-100 | 18 | |
| α-helix | 107-120 | 14 | |
| α-helix | 125-144 | 20 | |
| α-helix | 151-164 | 14 | |
| α-helix | 167-173 | 7 | |
| α-helix | 177-182 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 81-100 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2 homologous antagonist/killer | A | protein | 166 | Homo sapiens | Q16611 (AlphaFold model) |
| BH3-interacting domain death agonist p15 | B | protein | 22 | Homo sapiens | P55957 (AlphaFold model) |
>7M5A_1 Bcl-2 homologous antagonist/killer (chains A) SASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAI IGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLAL HVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLCNG
>7M5A_2 BH3-interacting domain death agonist p15 (chains B) EDIIRNIARHLAQWGDSMDRSW
Structural basis of BAK activation in mitochondrial apoptosis initiation. Singh, G., Guibao, C.D., Seetharaman, J. et al. Nat Commun (2022) 13:250-250. DOI 10.1038/s41467-021-27851-y · 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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