Mitotic spindle assembly checkpoint protein MAD2B (MAD2L2) is a 211-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UI95.
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The mean pLDDT of this model is 90.4 (very high 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 | 74% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Adapter protein able to interact with different proteins and involved in different biological processes (PubMed:11459825, PubMed:11459826, PubMed:17296730, PubMed:17719540, PubMed:19443654, PubMed:29656893). Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis (PubMed:20164194, PubMed:23143872). Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions (PubMed:20164194). Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks…
Homooligomer (Probable). Heterodimer with REV3L (PubMed:10660610, PubMed:11485998, PubMed:23143872). This dimer forms the minimal DNA polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA polymerase catalytic activity, although its activity is very low in this context (PubMed:11485998). Component of the tetrameric Pol-zeta complex (Pol-zeta4), which consists of REV3L, MAD2L2, POLD2 and…
Nucleus, Cytoplasm, cytoskeleton, spindle, Cytoplasm, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6BCD | X-ray | 1.43 Å | A=1-211 |
| 6BC8 | X-ray | 1.68 Å | A=1-211 |
| 6M7B | X-ray | 1.77 Å | A/B=1-211 |
| 3ABD | X-ray | 1.9 Å | A/B=1-211 |
| 4EXT | X-ray | 1.9 Å | C=7-209 |
| 6M7A | X-ray | 1.9 Å | A/B=1-208 |
| 6NIF | X-ray | 2.0 Å | A=2-211 |
| 6VE5 | X-ray | 2.0 Å | A=1-211 |
| 5XPT | X-ray | 2.1 Å | A=1-211 |
| 6K07 | X-ray | 2.24 Å | A=7-211 |
| 6WS0 | X-ray | 2.24 Å | CCC=1-211 |
| 5XPU | X-ray | 2.3 Å | A=1-211 |
| 6K08 | X-ray | 2.31 Å | A=7-211 |
| 6KEA | X-ray | 2.35 Å | A/B/C/D=12-211 |
| 6WS5 | X-ray | 2.47 Å | CCC=1-211 |
| 3ABE | X-ray | 2.6 Å | C=1-211 |
| 4GK0 | X-ray | 2.7 Å | A/B=1-211 |
| 6WW9 | X-ray | 2.7 Å | A/B=2-211 |
| 3VU7 | X-ray | 2.8 Å | C=1-211 |
| 6BI7 | X-ray | 2.8 Å | A/C/E/G=1-211 |
Showing 20 of 24 experimental structures (best resolution first).
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