Fibronectin (FN1) is a 2477-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02751.
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The mean pLDDT of this model is 69.6 (low 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 | 5% |
| 70 to 90 | Confident: backbone generally right | 56% |
| 50 to 70 | Low: treat with caution | 23% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). Acts as a ligand for the LILRB4 receptor, inhibiting FCGR1A/CD64-mediated…
Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP (PubMed:12225811). Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain); this interaction enhances fibronectin…
Secreted, extracellular space, extracellular matrix, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2CG7 | X-ray | 1.2 Å | A=93-182 |
| 4LXO | X-ray | 1.42 Å | A/B=1448-1631 |
| 5DC4 | X-ray | 1.48 Å | B=1536-1631 |
| 2CG6 | X-ray | 1.55 Å | A=93-182 |
| 5DC9 | X-ray | 1.56 Å | B=1536-1631 |
| 5N48 | X-ray | 1.6 Å | B/D=1266-1357 |
| 3CAL | X-ray | 1.7 Å | A/C=93-182 |
| 3ZRZ | X-ray | 1.7 Å | A/B=93-182 |
| 6MFA | X-ray | 1.75 Å | A=903-1268 |
| 1FNA | X-ray | 1.8 Å | A=1543-1633 |
| 2RKY | X-ray | 1.8 Å | A/C=183-275 |
| 4PZ5 | X-ray | 1.96 Å | A=93-182 |
| 1FNF | X-ray | 2.0 Å | A=1173-1631 |
| 2CK2 | X-ray | 2.0 Å | A/B=1538-1633 |
| 2RKZ | X-ray | 2.0 Å | A/B/C/D/E/F=93-182 |
| 2RL0 | X-ray | 2.0 Å | A/B/D/F/I/K=184-272 |
| 2GEE | X-ray | 2.01 Å | A=1266-1447 |
| 3EJH | X-ray | 2.1 Å | A/B=516-608 |
| 5DC0 | X-ray | 2.23 Å | A=1538-1631 |
| 4JEG | X-ray | 2.3 Å | B=1538-1631 |
Showing 20 of 65 experimental structures (best resolution first).
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