E3 ubiquitin-protein ligase AMFR (AMFR) is a 643-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UKV5.
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The mean pLDDT of this model is 72.8 (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 | 27% |
| 70 to 90 | Confident: backbone generally right | 38% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins, such as CD3D, CYP3A4, CFTR, INSIG1, SOAT2/ACAT2 and APOB for proteasomal degradation (PubMed:10456327, PubMed:11724934, PubMed:12670940, PubMed:19103148, PubMed:24424410, PubMed:28604676). Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD) (PubMed:10456327, PubMed:11724934, PubMed:19103148, PubMed:24424410). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG1 complex at the ER membrane (PubMed:16168377,…
Interacts with RNF5 (By similarity). Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 and RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation (By similarity). Interacts with DERL1 (PubMed:16186510). Interacts (through a region distinct from the RING finger) with UBE2G2/UBC7 (PubMed:11724934). Component of the VCP/p97-AMFR/gp78 complex that…
Endoplasmic reticulum membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4G3O | X-ray | 1.6 Å | A=456-498 |
| 3H8K | X-ray | 1.8 Å | B=573-600 |
| 3TIW | X-ray | 1.8 Å | C/D=622-640 |
| 8T0S | X-ray | 1.95 Å | B=574-600 |
| 4LAD | X-ray | 2.3 Å | B=313-393, B=574-600 |
| 3FSH | X-ray | 2.76 Å | C=574-601 |
| 2EJS | NMR | A=452-502 | |
| 2LVN | NMR | C=453-504 | |
| 2LVO | NMR | C=453-504 | |
| 2LVP | NMR | C=453-504 | |
| 2LVQ | NMR | D=453-504 | |
| 2LXH | NMR | C=313-393 | |
| 2LXP | NMR | B=574-600, C=327-384 |
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