E3 ubiquitin-protein ligase Mdm2 (MDM2) is a 491-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q00987.
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The mean pLDDT of this model is 62.6 (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 | 30% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 14% |
| Below 50 | Very low: often disordered regions | 48% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed:29681526, PubMed:21317885). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which…
Component of a ternary complex composed of FAM193A, MDM4 and MDM2; interaction of FAM193A with MDM4 is mediated by the MDM4 RING-type zinc finger and results in MDM4 destabilization, leading to enhanced p53/TP53 transcriptional activity (PubMed:36897777). Although FAM193A interacts with MDM4 and MDM2, it does not affect formation of the p53-MDM2-MDM4 transcriptional repressor complex…
Nucleus, nucleoplasm, Cytoplasm, Nucleus, nucleolus, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6Q9L | X-ray | 1.13 Å | A/B=17-111 |
| 5C5A | X-ray | 1.15 Å | A/B=20-111 |
| 6Q9O | X-ray | 1.21 Å | A/B=17-111 |
| 5ZXF | X-ray | 1.25 Å | A=24-110 |
| 7QDQ | X-ray | 1.26 Å | A=20-111 |
| 8F10 | X-ray | 1.28 Å | A=17-111 |
| 8P0D | X-ray | 1.31 Å | B=161-191 |
| 5Z02 | X-ray | 1.35 Å | A=24-112 |
| 8J81 | X-ray | 1.35 Å | A=17-111 |
| 4OGN | X-ray | 1.38 Å | A=6-110 |
| 2AXI | X-ray | 1.4 Å | A=17-125 |
| 7KJM | X-ray | 1.4 Å | A/C=25-109 |
| 8F13 | X-ray | 1.4 Å | A=17-111 |
| 6SQO | X-ray | 1.41 Å | A/D=430-491 |
| 4WT2 | X-ray | 1.42 Å | A=6-110 |
| 4UE1 | X-ray | 1.45 Å | A/B/C/D=17-125 |
| 7NUS | X-ray | 1.45 Å | A/B/C=17-111 |
| 8PWC | X-ray | 1.46 Å | A/B/C=17-125 |
| 8GCG | X-ray | 1.47 Å | A=17-125 |
| 4OGT | X-ray | 1.54 Å | A=6-110 |
Showing 20 of 147 experimental structures (best resolution first).
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