Insulin-degrading enzyme (IDE) is a 1019-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P14735.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 94.0 (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 | 93% |
| 70 to 90 | Confident: backbone generally right | 1% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed:10684867, PubMed:17051221, PubMed:17613531, PubMed:18986166, PubMed:19321446, PubMed:21098034, PubMed:2293021, PubMed:23922390, PubMed:24847884, PubMed:26394692, PubMed:26968463, PubMed:29596046). Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (PubMed:23922390, PubMed:26394692, PubMed:29596046). Contributes to the regulation of peptide hormone signaling cascades and regulation of blood…
Homodimer (Probable) (PubMed:17051221, PubMed:19321446, PubMed:23922390, PubMed:26394692, PubMed:29596046). Can also form homotetramers (By similarity)
Cytoplasm, cytosol, Cell membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3CWW | X-ray | 1.96 Å | A/B=42-1019 |
| 2G47 | X-ray | 2.1 Å | A/B=42-1019 |
| 2G56 | X-ray | 2.2 Å | A/B=42-1019 |
| 4PES | X-ray | 2.21 Å | A/B=42-1019 |
| 4PFC | X-ray | 2.21 Å | A/B=42-1019 |
| 2G54 | X-ray | 2.25 Å | A/B=42-1019 |
| 3E4Z | X-ray | 2.28 Å | A/B=42-1019 |
| 3E50 | X-ray | 2.3 Å | A/B=42-1019 |
| 4PF7 | X-ray | 2.33 Å | A/B=42-1019 |
| 3OFI | X-ray | 2.35 Å | A/B=42-1019 |
| 2G49 | X-ray | 2.5 Å | A/B=42-1019 |
| 4PF9 | X-ray | 2.5 Å | A/B=42-1019 |
| 2WK3 | X-ray | 2.59 Å | A/B=1-1019 |
| 2G48 | X-ray | 2.6 Å | A/B=42-1019 |
| 2WBY | X-ray | 2.6 Å | A/B=42-1019 |
| 3E4A | X-ray | 2.6 Å | A/B=1-1019 |
| 7K1F | X-ray | 2.6 Å | A/B=42-1019 |
| 4GSF | X-ray | 2.7 Å | A/B=42-1019 |
| 4LTE | X-ray | 2.7 Å | A/B=42-1019 |
| 4NXO | X-ray | 2.73 Å | A/B=42-1019 |
Showing 20 of 62 experimental structures (best resolution first).
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