2XPX: BHRF1:Bak BH3 complex

Crystal structure of BHRF1:Bak BH3 complex. Determined by X-ray diffraction at 2.05 Å resolution. Released 26 Jan 2011.

Method
X-ray diffraction
Resolution
2.05 Å
Organisms
HUMAN HERPESVIRUS 4, HOMO SAPIENS
Chains
2
Atoms
1,534
Mol. weight
23.1 kDa
Released
26 Jan 2011

Explore 2XPX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix5-2016
α-helix27-359
α-helix45-6016
α-helix62-7514
α-helix79-9113
α-helix98-11720
α-helix123-13715
α-helix138-1403
α-helix141-1466
α-helix150-1556
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix70-8920

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator BHRF1Aprotein173HUMAN HERPESVIRUS 4P03182 (AlphaFold model)
Bcl-2 homologous antagonist/killerBprotein26HOMO SAPIENSQ16611 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2XPX_1 APOPTOSIS REGULATOR BHRF1 (chains A)
MGSHHHHHHSQDPMAYSTREILLALCIRDSRVHGNGTLHPVLELAARETPLRLSPEDTVV
LRYHVLLEEIIERNSETFTETWNRFITHTEHVDLDFNSVFLEIFHRGDPSLGRALAWMAW
CMHACRTLCCNQSTPYYVVDLSVRGMLEASEGLDGWIHQQGGWSTLIEDNIPG
Sequence of entity 2 (B), FASTA
>2XPX_2 BCL-2 HOMOLOGOUS ANTAGONIST/KILLER (chains B)
PSSTMGQVGRQLAIIGDDINRRYDSE

Primary citation

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:

Browse structure collections

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