Q00653: Nuclear factor NF-kappa-B p100 subunit (NFKB2)

Nuclear factor NF-kappa-B p100 subunit (NFKB2) is a 900-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q00653.

Gene
NFKB2
Organism
Homo sapiens
Length
900 residues
Mean pLDDT
74.9
Model
AF-Q00653-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.9 (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 accurate38%
70 to 90Confident: backbone generally right34%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions24%

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 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…

Subunit structure

Component of the NF-kappa-B RelB-p52 complex. Homodimer; component of the NF-kappa-B p52-p52 complex. Component of the NF-kappa-B p65-p52 complex. Component of the NF-kappa-B p52-c-Rel complex. NFKB2/p52 interacts with NFKBIE. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Directly interacts with MEN1

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
1A3QX-ray2.1 ÅA/B=37-327
8G8SX-ray2.1 ÅB=309-343
8G8QX-ray2.6 ÅB=332-348
5ZMCX-ray2.99 ÅA=35-329
7CLIX-ray3.0 ÅA/B=1-398
7W7LX-ray3.0 ÅA/B=1-327
3DO7X-ray3.05 ÅB=37-329
7VUQX-ray3.1 ÅA/B=1-398
4OT9X-ray3.35 ÅA=407-765
7VUPX-ray3.4 ÅA/B=1-398
2D96NMRA=766-859

More AlphaFold highlights

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