Nuclear factor NF-kappa-B p105 subunit (Nfkb1) is a 971-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P25799.
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The mean pLDDT of this model is 73.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 46% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 27% |
What pLDDT means and how to read it
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 and the heterodimeric p65-p50 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…
Component of the NF-kappa-B p65-p50 complex (By similarity). Homodimer; component of the NF-kappa-B p50-p50 complex (By similarity). Component of the NF-kappa-B p105-p50 complex (By similarity). Component of the NF-kappa-B p50-c-Rel complex (By similarity). Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By similarity). Also interacts with MAP3K8 (By similarity).…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1U36 | X-ray | 1.89 Å | A=245-350 |
| 1U3J | X-ray | 1.9 Å | A=245-350 |
| 1U3Y | X-ray | 1.9 Å | A=245-350 |
| 1U3Z | X-ray | 1.9 Å | A=245-350 |
| 9BOR | X-ray | 2.0 Å | B/C=245-376 |
| 1BFS | X-ray | 2.2 Å | A=245-350 |
| 1U41 | X-ray | 2.2 Å | A/B/C/D=245-350 |
| 1IKN | X-ray | 2.3 Å | C=245-363 |
| 1NFK | X-ray | 2.3 Å | A/B=39-363 |
| 1OOA | X-ray | 2.45 Å | A/B=39-363 |
| 1LEI | X-ray | 2.7 Å | B=39-350 |
| 1U42 | X-ray | 2.7 Å | A=245-350 |
| 1LE5 | X-ray | 2.75 Å | B/F=39-350 |
| 2I9T | X-ray | 2.8 Å | B=39-350 |
| 8TKM | X-ray | 2.8 Å | A/B=39-350 |
| 8TKN | X-ray | 2.8 Å | A/B=39-350 |
| 1VKX | X-ray | 2.9 Å | B=39-350 |
| 1LE9 | X-ray | 3.0 Å | B/F=39-350 |
| 8TKL | X-ray | 3.0 Å | A/B=39-350 |
| 2V2T | X-ray | 3.05 Å | B=38-363 |
Showing 20 of 21 experimental structures (best resolution first).
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