Ubiquitin carboxyl-terminal hydrolase 7 (USP7) is a 1102-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q93009.
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The mean pLDDT of this model is 86.3 (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 | 63% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Hydrolase that deubiquitinates target proteins such as ARMC5, FOXO4, DEPTOR, KAT5, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148, PubMed:25865756, PubMed:26678539, PubMed:28655758, PubMed:33544460, PubMed:35216969). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell…
Monomer. Homodimer. Part of a complex with DAXX, MDM2, RASSF1 and USP7 (PubMed:18566590). Part of a complex with DAXX, MDM2 and USP7 (PubMed:16845383). Interacts with MDM2; the interaction is independent of p53/TP53. Interacts with DAXX; the interaction is direct and independent of MDM2 and p53/TP53 (PubMed:16845383). Component of a complex composed of KMT2E/MLL5 (isoform 3), OGT (isoform 1) and…
Nucleus, Cytoplasm, Nucleus, PML body, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4YSI | X-ray | 1.02 Å | A=63-205 |
| 5KYC | X-ray | 1.43 Å | B=208-554 |
| 5KYF | X-ray | 1.45 Å | B=208-554 |
| 2FOJ | X-ray | 1.6 Å | A=54-205 |
| 2XXN | X-ray | 1.6 Å | A=63-205 |
| 5KYD | X-ray | 1.62 Å | A=208-554 |
| 2F1W | X-ray | 1.65 Å | A=53-206 |
| 1YY6 | X-ray | 1.7 Å | A=54-205 |
| 2F1Y | X-ray | 1.7 Å | A=53-207 |
| 4KG9 | X-ray | 1.7 Å | A=54-205 |
| 5N9T | X-ray | 1.73 Å | A/B=207-560 |
| 9DEM | X-ray | 1.77 Å | A=208-554 |
| 3MQR | X-ray | 1.8 Å | A=54-205 |
| 5VSB | X-ray | 1.85 Å | A/B=208-560 |
| 4JJQ | X-ray | 1.95 Å | A=54-207 |
| 5KYE | X-ray | 1.97 Å | A/B=208-554 |
| 1YZE | X-ray | 2.0 Å | A/B/C=54-205 |
| 9DEK | X-ray | 2.0 Å | A/B=208-554 |
| 2FOP | X-ray | 2.1 Å | A=54-205 |
| 7XHH | X-ray | 2.1 Å | A/B=207-554 |
Showing 20 of 82 experimental structures (best resolution first).
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