P03206: Lytic switch protein BZLF1 (BZLF1)

Lytic switch protein BZLF1 (BZLF1) is a 245-residue protein from Epstein-Barr virus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P03206.

Gene
BZLF1
Organism
Epstein-Barr virus
Length
245 residues
Mean pLDDT
53.7
Model
AF-0000000365833927 v1
Model created
3 Jul 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 53.7 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate8%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions58%

What pLDDT means and how to read it

Function

Transcription factor that acts as a molecular switch to induce the transition from the latent to the lytic or productive phase of the virus cycle (Probable) (PubMed:8404860). Mediates the switch from the latent to the lytic cycle of infection in cells containing a highly methylated viral genome (PubMed:15361873, PubMed:34893887). Probably binds to silenced chromatin and recruits host chromatin-remodeling enzymes (PubMed:30926617). Regulates this switch by binding to 2 types of ZEBRA response elements (ZREs): the CpG-free AP-1 like elements (latency) and the methylated CpG-containing elements (lytic replication) (Probable) (PubMed:22022468, PubMed:34893887). Activates preferentially the…

Subunit structure

Homodimer (PubMed:11333921, PubMed:15078966, PubMed:28158710). Interacts (via b-ZIP domain) with the DNA polymerase processivity factor BMRF1 (via N-terminus); this interaction may inhibit BZLF1-induced transcription of the BMRF1 promoter (PubMed:8764021). Interacts with human UBN1, CRTC2 and RACK1 (PubMed:10725330, PubMed:10849009, PubMed:19164291). Interacts (via N-terminus) with human PAX5…

Subcellular location

Host nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3SPVX-ray1.3 ÅC=190-197
3VFNX-ray1.5 ÅC=52-64
1ZSDX-ray1.7 ÅC=54-64
3VFOX-ray1.7 ÅC=52-64
2AXFX-ray1.8 ÅC=77-86
3VFPX-ray1.85 ÅC=52-64
3VFRX-ray1.85 ÅC=52-64
2AXGX-ray2.0 ÅC=77-86
3KWWX-ray2.18 ÅC=52-64
2C9LX-ray2.25 ÅY/Z=175-236
5SZXX-ray2.25 ÅA/B=175-236
2AK4X-ray2.5 ÅC/H/M/S=52-64
7NX5X-ray2.5 ÅA/B/E/F=175-236
2NX5X-ray2.7 ÅC/H/M/S=54-64
3KXFX-ray3.1 ÅQ/R/S/T=52-64
2C9NX-ray3.3 ÅY/Z=175-236

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