Q04863: Transcription factor RelB (Relb)

Transcription factor RelB (Relb) is a 558-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q04863.

Gene
Relb
Organism
Mus musculus
Length
558 residues
Mean pLDDT
68.3
Model
AF-Q04863-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.3 (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 accurate42%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions40%

What pLDDT means and how to read it

Function

NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B…

Subunit structure

Component of the NF-kappa-B RelB-p50 complex. Component of the NF-kappa-B RelB-p52 complex (By similarity). Self-associates; the interaction seems to be transient and may prevent degradation allowing for heterodimer formation p50 or p52. Interacts with NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with NFKBID. Interacts with BMAL1 and the interaction is enhanced in the presence of CLOCK

Subcellular location

Nucleus, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1ZK9X-ray2.18 ÅA=276-378
1ZKAX-ray2.2 ÅA=276-378
4JHBX-ray2.44 ÅA=277-378
3JUZX-ray2.51 ÅA=278-378
3JSSX-ray2.6 ÅA=278-378
3JV0X-ray2.65 ÅA=278-378
3JV6X-ray2.78 ÅA/C/E=278-378
4JGMX-ray3.0 ÅA=277-378
2V2TX-ray3.05 ÅA=91-378
3DO7X-ray3.05 ÅA=88-383
3JV4X-ray3.15 ÅA/C/E=278-378

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