Crystal structure of a computationally designed inhibitor of an Epstein-Barr viral Bcl-2 protein. Determined by X-ray diffraction at 1.8 Å resolution. Released 9 Jul 2014.
Explore 4OYD in 3D Show helices and sheets RCSB PDB PDBe
4OYD contains 29 α-helices and 0 β-strands across 4 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 | 5-17 | 13 | |
| α-helix | 24-26 | 3 | |
| α-helix | 27-35 | 9 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-73 | 12 | |
| 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 | 149-153 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-32 | 30 | |
| α-helix | 39-76 | 38 | |
| α-helix | 82-116 | 35 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-18 | 14 | |
| α-helix | 24-26 | 3 | |
| α-helix | 27-35 | 9 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-73 | 12 | |
| 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 | 149-153 | 5 | |
| α-helix | 155-157 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator BHRF1 | A, C | protein | 158 | Epstein-Barr virus | P0C6Z1 |
| Computationally designed Inhibitor | B, D | protein | 117 | synthetic construct |
>4OYD_1 Apoptosis regulator BHRF1 (chains A, C) SAYSTREILLALCIRDSRVHGNGTLHPVLELAARETPLRLSPEDTVVLRYHVLLEEIIER NSETFTETWNRFITHTEHVDLDFNSVFLEIFHRGDPSLGRALAWMAWCMHACRTLCCNQS TPYYVVDLSVRGMLEASEGLDGWIHQQGGWSTLIEDNI
>4OYD_2 Computationally designed Inhibitor (chains B, D) ADPKKVLDKAKDQAENRVRELKQKLEELYKEARKLDLTQEMRRKLELRYIAAMLMAIGDI YNAIRQAKQEADKLKKAGLVNSQQLDELKRRLEELKEEASRKARDYGREFQLKLEYG
A computationally designed inhibitor of an epstein-barr viral bcl-2 protein induces apoptosis in infected cells. Procko, E., Berguig, G.Y., Shen, B.W. et al. Cell (2014) 157:1644-1656. DOI 10.1016/j.cell.2014.04.034 · PubMed
Other PDB entries of the same protein (UniProt P0C6Z1), best resolution first:
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