Ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) is a 167-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y3C8.
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The mean pLDDT of this model is 93.4 (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 | 88% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
E2-like enzyme which specifically catalyzes the second step in ufmylation (PubMed:15071506, PubMed:29868776, PubMed:30626644, PubMed:34588452, PubMed:35394863, PubMed:36121123, PubMed:38383789). Accepts the ubiquitin-like modifier UFM1 from the E1 enzyme UBA5 and forms an intermediate with UFM1 via a thioester linkage (PubMed:15071506, PubMed:29868776, PubMed:34588452, PubMed:38383789). Ufmylation is involved in various processes, such as ribosome recycling, response to DNA damage, interferon response or reticulophagy (also called ER-phagy) (PubMed:27351204, PubMed:32160526, PubMed:35394863, PubMed:37036982, PubMed:38383789)
Interacts with UBA5 (via C-terminus) (PubMed:17825256, PubMed:27653677, PubMed:29868776, PubMed:34588452). Interacts with UFL1 (PubMed:20018847, PubMed:30886146, PubMed:37988244, PubMed:38383789). Interacts with UFM1 (PubMed:29868776). Interacts with KIRREL3 (PubMed:25902260)
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9GLH | X-ray | 1.11 Å | AAA=1-167 |
| 9GLJ | X-ray | 1.21 Å | AAA=1-167 |
| 9GMM | X-ray | 1.35 Å | AAA=1-167 |
| 9GLI | X-ray | 1.43 Å | AAA=1-167 |
| 9GLO | X-ray | 1.53 Å | AAA=1-167 |
| 9I9M | X-ray | 1.54 Å | AAA=1-167 |
| 2Z6O | X-ray | 1.6 Å | A=1-167 |
| 9GLL | X-ray | 1.65 Å | AAA=1-167 |
| 9GLP | X-ray | 1.77 Å | AAA=1-167 |
| 8BZR | X-ray | 1.78 Å | A=1-167 |
| 9GLM | X-ray | 1.79 Å | AAA=1-167 |
| 2Z6P | X-ray | 1.8 Å | A=1-167 |
| 9I9N | X-ray | 1.88 Å | AAA=1-167 |
| 9IA8 | X-ray | 1.9 Å | AAA=1-167 |
| 9GLN | X-ray | 1.92 Å | AAA=1-167 |
| 7NW1 | X-ray | 1.95 Å | AAA/BBB=1-167 |
| 9GN8 | X-ray | 1.96 Å | AAA=1-167 |
| 9GMN | X-ray | 2.0 Å | AAA=1-167 |
| 9I9P | X-ray | 2.02 Å | AAA=1-167 |
| 9GLK | X-ray | 2.03 Å | AAA=1-167 |
Showing 20 of 27 experimental structures (best resolution first).
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