Crystal structure of BHRF1:Bak BH3 complex. Determined by X-ray diffraction at 2.05 Å resolution. Released 26 Jan 2011.
Explore 2XPX in 3D Show helices and sheets RCSB PDB PDBe
2XPX 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 | 5-20 | 16 | |
| α-helix | 27-35 | 9 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-75 | 14 | |
| α-helix | 79-91 | 13 | |
| α-helix | 98-117 | 20 | |
| α-helix | 123-137 | 15 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-146 | 6 | |
| α-helix | 150-155 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 70-89 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator BHRF1 | A | protein | 173 | HUMAN HERPESVIRUS 4 | P03182 (AlphaFold model) |
| Bcl-2 homologous antagonist/killer | B | protein | 26 | HOMO SAPIENS | Q16611 (AlphaFold model) |
>2XPX_1 APOPTOSIS REGULATOR BHRF1 (chains A) MGSHHHHHHSQDPMAYSTREILLALCIRDSRVHGNGTLHPVLELAARETPLRLSPEDTVV LRYHVLLEEIIERNSETFTETWNRFITHTEHVDLDFNSVFLEIFHRGDPSLGRALAWMAW CMHACRTLCCNQSTPYYVVDLSVRGMLEASEGLDGWIHQQGGWSTLIEDNIPG
>2XPX_2 BCL-2 HOMOLOGOUS ANTAGONIST/KILLER (chains B) PSSTMGQVGRQLAIIGDDINRRYDSE
Structural Basis for Apoptosis Inhibition by Epstein-Barr Virus Bhrf1. Kvansakul, M., Wei, A.H., Fletcher, J.I. et al. PLoS Pathog (2010) 6:1236. DOI 10.1371/JOURNAL.PPAT.1001236 · PubMed
Other PDB entries of the same protein (UniProt P03182 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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