Proteasomal ubiquitin receptor ADRM1 (ADRM1) is a 407-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16186.
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The mean pLDDT of this model is 62.3 (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 | 16% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 33% |
| Below 50 | Very low: often disordered regions | 35% |
What pLDDT means and how to read it
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Therefore, the proteasome participates in numerous cellular processes, including…
Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP) (PubMed:16990800). Interacts with the proteasomal scaffolding protein PSMD1 (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:20471946). Interacts with deubiquitinase UCHL5; this interaction activates the auto-inhibited UCHL5 by…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5V1Y | X-ray | 1.42 Å | A/B=19-132 |
| 6OI4 | X-ray | 1.76 Å | A/B=20-132 |
| 5IRS | X-ray | 1.8 Å | A=2-150 |
| 8VWO | X-ray | 1.85 Å | A=1-150 |
| 4WLR | X-ray | 2.0 Å | B=285-386 |
| 5V1Z | X-ray | 2.0 Å | A/B=19-132 |
| 8FTQ | X-ray | 2.1 Å | A/B=2-150 |
| 4UEL | X-ray | 2.3 Å | C=266-388 |
| 9E7K | X-ray | 2.41 Å | B=269-388 |
| 4UEM | X-ray | 2.82 Å | B=266-388 |
| 4WLQ | X-ray | 2.85 Å | B=286-384 |
| 2KQZ | NMR | A=253-407 | |
| 2KR0 | NMR | A=1-407 | |
| 2L5V | NMR | A=260-407 | |
| 2MKZ | NMR | A=270-407 | |
| 2NBV | NMR | A=1-150 | |
| 5YMY | NMR | C=1-150 | |
| 6CO4 | NMR | A=1-150 | |
| 6UYI | NMR | A=1-150 | |
| 6UYJ | NMR | A=1-150 |
Showing 20 of 21 experimental structures (best resolution first).
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