Menin (MEN1) is a 610-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00255.
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The mean pLDDT of this model is 84.4 (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 | 73% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 20% |
What pLDDT means and how to read it
Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be involved in normal hematopoiesis through the activation of HOXA9 expression (By similarity). May be involved in DNA repair
Component of the MLL-HCF complex, at least composed of KMT2A/MLL1, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2. Component of the menin-associated histone methyltransferase complex, at least composed of KMT2B/MLL4, MEN1, ASH2L, RBBP5, DPY30 and WDR5. Interacts with POLR2B. Interacts with POLR2A phosphorylated at 'Ser-5', but not with the unphosphorylated, nor 'Ser-2' phosphorylated POLR2A…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6O5I | X-ray | 1.24 Å | A=1-593 |
| 4GQ4 | X-ray | 1.27 Å | A=1-593 |
| 8VA5 | X-ray | 1.3 Å | A=1-593 |
| 9C4Y | X-ray | 1.31 Å | A=1-593 |
| 9C4W | X-ray | 1.4 Å | A=1-593 |
| 9C4Z | X-ray | 1.4 Å | A=1-593 |
| 4OG4 | X-ray | 1.45 Å | A=1-593 |
| 4GPQ | X-ray | 1.46 Å | A=1-593 |
| 9C4T | X-ray | 1.46 Å | A=1-593 |
| 9C4V | X-ray | 1.47 Å | A=1-593 |
| 4OG6 | X-ray | 1.49 Å | A=1-593 |
| 5DB0 | X-ray | 1.5 Å | A=1-593 |
| 6OPJ | X-ray | 1.5 Å | A=1-593 |
| 9WN9 | X-ray | 1.5 Å | A/B=2-583 |
| 4OG8 | X-ray | 1.53 Å | A=1-593 |
| 5DB2 | X-ray | 1.54 Å | A=1-593 |
| 5DDB | X-ray | 1.54 Å | A=1-593 |
| 9C4S | X-ray | 1.54 Å | A=1-593 |
| 4GQ6 | X-ray | 1.55 Å | A=1-593 |
| 4GQ3 | X-ray | 1.56 Å | A=1-593 |
Showing 20 of 69 experimental structures (best resolution first).
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