Human BAK in complex with the dF2 peptide. Determined by X-ray diffraction at 1.3 Å resolution. Released 11 Jan 2023.
Explore 8CZF in 3D Show helices and sheets RCSB PDB PDBe
8CZF contains 11 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 | 21-23 | 3 | |
| α-helix | 24-45 | 22 | |
| α-helix | 55-57 | 3 | |
| α-helix | 58-61 | 4 | |
| 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 | 177-181 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-21 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2 homologous antagonist/killer | A | protein | 170 | Homo sapiens | Q16611 (AlphaFold model) |
| DF2 peptide | B | protein | 24 | synthetic construct |
>8CZF_1 Bcl-2 homologous antagonist/killer (chains A) GPLGSMSEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGR QLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGY RLALHVYQHGLTGFLGQVTRFVVDFMLHHSIARWIAQRGGWVAALNLGNG
>8CZF_2 DF2 peptide (chains B) XSYIDKIADLIRKVAEEINSKLEX
Peptides from human BNIP5 and PXT1 and non-native binders of pro-apoptotic BAK can directly activate or inhibit BAK-mediated membrane permeabilization. Aguilar, F., Yu, S., Grant, R.A. et al. Structure (2023) 31:265-281.e7. DOI 10.1016/j.str.2023.01.001 · 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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