Centromere protein M (CENPM) is a 180-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NSP4.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 89.2 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 70% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres
Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS
Nucleus, Cytoplasm, Chromosome, centromere, kinetochore
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4P0T | X-ray | 1.49 Å | A/B=1-171 |
| 4WAU | X-ray | 2.2 Å | A/B=1-171 |
| 7R5S | EM | 2.83 Å | M=1-180 |
| 7PKN | EM | 3.2 Å | M=1-180 |
| 7XHO | EM | 3.29 Å | M=1-180 |
| 7XHN | EM | 3.71 Å | M=1-180 |
| 7R5V | EM | 4.55 Å | M=1-180 |
| 7QOO | EM | 4.6 Å | M=1-180 |
| 7YYH | EM | 8.9 Å | M=1-180 |
| 7YWX | EM | 12.0 Å | M=1-180 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.