1Q59: Early antigen protein R

Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2. Determined by solution NMR. Released 23 Sept 2003.

Method: Solution NMR
Organism: Human herpesvirus 4
Chains: 1
Atoms: 1,395
Mol. weight: 19.85 kDa
Released: 23 Sept 2003

Explore 1Q59 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Q59 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.

Chain A: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	8-18	11
α-helix	45-60	16
α-helix	62-72	11
α-helix	81-89	9
α-helix	99-117	19
α-helix	122-137	16
α-helix	140-145	6
α-helix	153-156	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Early antigen protein R	A	protein	172	Human herpesvirus 4	P03182 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1Q59_1 Early antigen protein R (chains A)
MAYSTREILLALCIRDSRVHGNGTLHPVLELAARETPLRLSPEDTVVLRYHVLLEEIIER
NSETFTETWNRFITHTEHVDLDFNSVFLEIFHRGDPSLGRALAWMAWCMHACRTLCCNQS
TPYYVVDLSVRGMLEASEGLDGWIHQQGGWSTLIEDNIPGDDDDLEHHHHHH

Primary citation

Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2. Huang, Q., Petros, A.M., Virgin, H.W. et al. J Mol Biol (2003) 332:1123-1130. DOI 10.1016/j.jmb.2003.08.007 · 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
7P33 2.79 Å, Epstein-Barr virus encoded Bcl-2 homolog BHRF-1 in complex with Bid BH3 peptide

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