Neutrophil gelatinase-associated lipocalin (LCN2) is a 198-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P80188.
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The mean pLDDT of this model is 91.3 (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 | 85% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (PubMed:12453413, PubMed:20581821, PubMed:27780864). Binds iron through association with 2,3-dihydroxybenzoic acid (2,3-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with…
Monomer (PubMed:1281792, PubMed:7683678). Homodimer; disulfide-linked (PubMed:7683678). Heterodimer; disulfide-linked with MMP9 (PubMed:7683678)
Secreted, Cytoplasmic granule lumen, Cytoplasmic vesicle lumen
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6GQZ | X-ray | 1.4 Å | A/B=25-198 |
| 4MVK | X-ray | 1.5 Å | A=21-198 |
| 5N48 | X-ray | 1.6 Å | A/C=21-198 |
| 4MVI | X-ray | 1.7 Å | A=21-198 |
| 6Z6Z | X-ray | 1.78 Å | A=21-198 |
| 6S8V | X-ray | 1.8 Å | A/C=21-198 |
| 6Z2C | X-ray | 1.8 Å | A/B/C=21-198 |
| 4IAX | X-ray | 1.9 Å | A=21-198 |
| 6QMU | X-ray | 1.98 Å | A/B=21-198 |
| 3DSZ | X-ray | 2.0 Å | A/B=21-198 |
| 5MHH | X-ray | 2.0 Å | A=21-198 |
| 8UYN | X-ray | 2.0 Å | A/B/C=21-198 |
| 4ZHC | X-ray | 2.04 Å | A/B/C=21-198 |
| 4ZHH | X-ray | 2.04 Å | A/B/C/D/E/F=21-198 |
| 4ZHD | X-ray | 2.05 Å | A/B/C=21-198 |
| 4ZHG | X-ray | 2.05 Å | A/B/C/D/E/F=21-198 |
| 8UZ9 | X-ray | 2.08 Å | A/B/C=21-198 |
| 1X71 | X-ray | 2.1 Å | A/B/C=21-198 |
| 1X89 | X-ray | 2.1 Å | A/B/C=21-198 |
| 4QAE | X-ray | 2.1 Å | A/B/C/D/E/F=21-198 |
Showing 20 of 59 experimental structures (best resolution first).
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