7P33: Epstein-Barr virus encoded Bcl-2 homolog BHRF-1
Epstein-Barr virus encoded Bcl-2 homolog BHRF-1 in complex with Bid BH3 peptide. Determined by X-ray diffraction at 2.79 Å resolution. Released 20 Jul 2022.
- Method
- X-ray diffraction
- Resolution
- 2.79 Å
- Organisms
- Epstein-Barr virus (strain B95-8), Homo sapiens
- Chains
- 10
- Atoms
- 7,263
- Mol. weight
- 117.86 kDa
- Ligands
- PO4
- Released
- 20 Jul 2022
Explore 7P33 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7P33 contains 64 α-helices and 0 β-strands across 10 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.
Chain A: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-19 | 15 | |
| α-helix | 24-26 | 3 | |
| α-helix | 27-34 | 8 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-75 | 14 | |
| α-helix | 79-91 | 13 | |
| α-helix | 98-116 | 19 | |
| α-helix | 123-136 | 14 | |
| α-helix | 137-140 | 4 | |
| α-helix | 141-147 | 7 | |
| α-helix | 150-155 | 6 | |
Chain B: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-19 | 15 | |
| α-helix | 24-26 | 3 | |
| α-helix | 27-34 | 8 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-74 | 13 | |
| α-helix | 79-91 | 13 | |
| α-helix | 95-97 | 3 | |
| α-helix | 98-116 | 19 | |
| α-helix | 123-136 | 14 | |
| α-helix | 137-140 | 4 | |
| α-helix | 141-146 | 6 | |
| α-helix | 150-154 | 5 | |
Chain C: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-19 | 15 | |
| α-helix | 27-34 | 8 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-73 | 12 | |
| α-helix | 79-91 | 13 | |
| α-helix | 95-97 | 3 | |
| α-helix | 98-116 | 19 | |
| α-helix | 123-137 | 15 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-146 | 6 | |
| α-helix | 150-154 | 5 | |
Chain D: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-19 | 15 | |
| α-helix | 25-26 | 2 | |
| α-helix | 27-35 | 9 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-72 | 11 | |
| α-helix | 79-90 | 12 | |
| α-helix | 95-97 | 3 | |
| α-helix | 98-116 | 19 | |
| α-helix | 123-136 | 14 | |
| α-helix | 137-140 | 4 | |
| α-helix | 141-144 | 4 | |
| α-helix | 145-147 | 3 | |
| α-helix | 149-155 | 7 | |
Chain E: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-19 | 15 | |
| α-helix | 24-26 | 3 | |
| α-helix | 27-34 | 8 | |
| α-helix | 45-60 | 16 | |
| α-helix | 62-73 | 12 | |
| α-helix | 79-90 | 12 | |
| α-helix | 98-116 | 19 | |
| α-helix | 123-137 | 15 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-145 | 5 | |
| α-helix | 149-152 | 4 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 80-95 | 16 | |
Chain G: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 79-98 | 20 | |
| α-helix | 101-105 | 5 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 79-96 | 18 | |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Apoptosis regulator BHRF1 | A, B, C, D, E | protein | 173 | Epstein-Barr virus (strain B95-8) | P03182 (AlphaFold model) |
| BH3-interacting domain death agonist p15 | F, G, H, I, J | protein | 34 | Homo sapiens | P55957 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>7P33_1 Apoptosis regulator BHRF1 (chains A, B, C, D, E)
MGSHHHHHHSQDPMAYSTREILLALCIRDSRVHGNGTLHPVLELAARETPLRLSPEDTVV
LRYHVLLEEIIERNSETFTETWNRFITHTEHVDLDFNSVFLEIFHRGDPSLGRALAWMAW
CMHACRTLCCNQSTPYYVVDLSVRGMLEASEGLDGWIHQQGGWSTLIEDNIPG
Sequence of entity 2 (F, G, H, I, J), FASTA
>7P33_2 BH3-interacting domain death agonist p15 (chains F, G, H, I, J)
SESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PO4 | Phosphate ion | O4 P | 1 |
Water and common crystallization additives (EDO) are not listed.
Primary citation
Crystal Structures of Epstein-Barr Virus Bcl-2 Homolog BHRF1 Bound to Bid and Puma BH3 Motif Peptides. Suraweera, C.D., Hinds, M.G., Kvansakul, M. Viruses (2022) 14. DOI 10.3390/v14102222 · PubMed
Other PDB entries of the same protein (UniProt P03182 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7P9W 2.0 Å, Epstein-Barr virus encoded apoptosis regulator BHRF1 in complex with Puma BH3
- 2XPX 2.05 Å, Crystal structure of BHRF1:Bak BH3 complex
- 8SM5 2.61 Å, Crystal Structure of BHRF1 from Epstein Barr Virus in complex with BID BH3 peptide
- 1Q59 Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
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