Protein fem-1 homolog B (FEM1B) is a 627-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UK73.
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The mean pLDDT of this model is 94.4 (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 | 84% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948, PubMed:33398168, PubMed:33398170). The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29779948, PubMed:33398168, PubMed:33398170). The CRL2(FEM1B) complex specifically recognizes proteins ending with -Gly-Leu-Asp-Arg, such as CDK5R1, leading to their…
Component of a CRL2 E3 ubiquitin-protein ligase complex, also named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter FEM1B (PubMed:15601820, PubMed:29779948). Homooligomer (PubMed:10542291). Interacts with PPM1F and PHTF1 (PubMed:11559703). Interacts with the death domain of FAS/TNFRSF6 and TNFRSF1A…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7EL6 | X-ray | 2.8 Å | A/B=1-337 |
| 9PW8 | X-ray | 2.8 Å | A/B=1-337 |
| 9PQA | X-ray | 2.9 Å | A/B=1-337 |
| 9PQ9 | X-ray | 2.93 Å | A/B=1-337 |
| 9PWJ | X-ray | 3.0 Å | A/B=1-337 |
| 9PXP | X-ray | 3.0 Å | A/B=1-337 |
| 9PXO | X-ray | 3.05 Å | A/B=1-337 |
| 9PQE | X-ray | 3.1 Å | A/B=1-337 |
| 6LBF | X-ray | 3.25 Å | A/B=1-356 |
| 8WQF | EM | 3.27 Å | F/J=1-627 |
| 8WQB | EM | 3.37 Å | F/J=1-627 |
| 8WQE | EM | 3.38 Å | B/D=1-627 |
| 8WQA | EM | 3.39 Å | B/D=1-627 |
| 8WQH | EM | 3.44 Å | D/H=1-627 |
| 7CNG | X-ray | 3.49 Å | A/B=1-337 |
| 8WQI | EM | 3.5 Å | D=1-627 |
| 8WQC | EM | 3.54 Å | A/G=1-627 |
| 8WQD | EM | 3.55 Å | D=1-627 |
| 9J77 | EM | 3.56 Å | F/J=1-627 |
| 9JCE | EM | 3.59 Å | A=1-627 |
Showing 20 of 31 experimental structures (best resolution first).
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