Midnolin (MIDN) is a 468-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q504T8.
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The mean pLDDT of this model is 64.9 (low 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 | 28% |
| 70 to 90 | Confident: backbone generally right | 16% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 43% |
What pLDDT means and how to read it
Facilitates the ubiquitin-independent proteasomal degradation of stimulus-induced transcription factors such as FOSB, EGR1, NR4A1, and IRF4 to the proteasome for degradation (PubMed:37616343). Promotes also the degradation of other substrates such as CBX4 (By similarity). Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion
Interacts with GCK; the interaction occurs preferentially at low glucose levels (PubMed:37616343). Interacts with the proteasome (PubMed:37616343)
Nucleus, nucleolus, Nucleus, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9VEH | X-ray | 2.0 Å | A=113-157, B=265-334 |
| 9VE3 | X-ray | 2.1 Å | A=111-157, B=265-334 |
| 9VE7 | X-ray | 2.15 Å | A=112-157, B=265-334 |
| 8VQP | X-ray | 2.52 Å | A=94-334 |
| 9VE4 | X-ray | 2.55 Å | A=111-157, B=265-334 |
| 9MBP | EM | 2.75 Å | f=1-468 |
| 9NKG | EM | 2.8 Å | z=1-468 |
| 9VE6 | X-ray | 2.8 Å | A=111-157, B=265-334 |
| 9MBO | EM | 2.83 Å | A=1-468 |
| 9VE8 | X-ray | 2.85 Å | A=112-157, B=265-334 |
| 9BV3 | EM | 2.9 Å | y=2-468 |
| 9NKI | EM | 2.94 Å | z=1-468 |
| 21IK | X-ray | 2.99 Å | A=111-157, B=265-334 |
| 9BV1 | EM | 3.1 Å | y=1-468 |
| 9VE5 | X-ray | 3.2 Å | A=111-157, B=265-334 |
| 21IE | X-ray | 3.24 Å | A=113-157, B=265-334 |
| 21IP | X-ray | 3.3 Å | A=111-157, B=265-334 |
| 9M2W | EM | 3.31 Å | u=1-468 |
| 9BV2 | EM | 3.4 Å | y=1-468 |
| 9UG9 | EM | 3.5 Å | u=1-468 |
Showing 20 of 23 experimental structures (best resolution first).
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