Q04206: Transcription factor p65 (RELA)

Transcription factor p65 (RELA) is a 551-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q04206.

Gene
RELA
Organism
Homo sapiens
Length
551 residues
Mean pLDDT
72.2
Model
AF-Q04206-F1 v6
Model created
1 Aug 2025
PDB structures
88

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.2 (confident 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 accurate47%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions34%

What pLDDT means and how to read it

Function

NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes 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 heterodimeric RELA-NFKB1 complex appears to be most abundant one. 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…

Subunit structure

Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-c-Rel complex. Homodimer; component of the NF-kappa-B p65-p65 complex. Component of the NF-kappa-B p65-p52 complex. May interact with ETHE1. Binds TLE5 and TLE1. Interacts with TP53BP2. Binds to and is phosphorylated by the activated form of either RPS6KA4 or RPS6KA5. Interacts with ING4 and this interaction may be…

Subcellular location

Nucleus, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6NV2X-ray1.13 ÅP=39-51
6QHLX-ray1.2 ÅP=38-51
7BI3X-ray1.2 ÅP=39-51
7BIQX-ray1.2 ÅP=39-51
7BIWX-ray1.2 ÅP=39-51
7NV4X-ray1.2 ÅP=39-51
7NVIX-ray1.2 ÅP=39-51
7NWSX-ray1.2 ÅP=39-51
7NXSX-ray1.2 ÅP=39-51
7NXTX-ray1.2 ÅP=39-51
7NXWX-ray1.2 ÅP=39-51
7NXYX-ray1.2 ÅP=39-51
7O34X-ray1.2 ÅP=39-51
7O3AX-ray1.2 ÅP=39-51
7O59X-ray1.2 ÅP=39-51
6YOWX-ray1.23 ÅP=39-51
7NQPX-ray1.24 ÅP=39-51
6QHMX-ray1.25 ÅP=275-287
7NSVX-ray1.33 ÅP=39-51
6YPYX-ray1.4 ÅP=39-51

Showing 20 of 88 experimental structures (best resolution first).

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