The crystal structure of BAK1 - a mitochondrial apoptosis regulator. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Jan 2007.
Explore 2JCN in 3D Show helices and sheets RCSB PDB PDBe
2JCN contains 8 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 | 24-47 | 24 | |
| α-helix | 58-60 | 3 | |
| α-helix | 70-100 | 31 | |
| α-helix | 107-118 | 12 | |
| α-helix | 125-144 | 20 | |
| α-helix | 151-164 | 14 | |
| α-helix | 167-173 | 7 | |
| α-helix | 177-182 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2 homologous antagonist/killer | A | protein | 172 | HOMO SAPIENS | Q16611 (AlphaFold model) |
>2JCN_1 BCL-2 HOMOLOGOUS ANTAGONIST/KILLER (chains A) SMSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQL AIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRL ALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILN
The Crystal Structure of Bak1 - an Apoptosis Trigger in the Mitochondrial Outer Membrane. Moche, M., Stenmark, P., Arrowsmith, C. et al. To be published.
Other PDB entries of the same protein (UniProt Q16611 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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