Fibrinogen alpha chain (FGA) is a 866-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02671.
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The mean pLDDT of this model is 60.3 (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 | 22% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 46% |
What pLDDT means and how to read it
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an…
Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5CFA | X-ray | 1.45 Å | C/D=580-594 |
| 4F27 | X-ray | 1.92 Å | Q=336-347 |
| 1FZD | X-ray | 2.1 Å | A/B/C/D/E/F/G/H=666-866 |
| 1BBR | X-ray | 2.3 Å | F/G/I=26-35 |
| 1FZC | X-ray | 2.3 Å | A/D=130-216 |
| 3E1I | X-ray | 2.3 Å | A/D=130-216 |
| 2OYH | X-ray | 2.4 Å | A/D=145-210 |
| 1RE3 | X-ray | 2.45 Å | A/D=145-210 |
| 1DM4 | X-ray | 2.5 Å | C=26-35 |
| 1FPH | X-ray | 2.5 Å | F=26-35 |
| 1FZG | X-ray | 2.5 Å | A/D=130-216 |
| 1YCP | X-ray | 2.5 Å | F/N=20-42 |
| 3AT0 | X-ray | 2.5 Å | B=332-347 |
| 1RF1 | X-ray | 2.53 Å | A/D=145-210 |
| 2HLO | X-ray | 2.6 Å | A/D=130-216 |
| 3BVH | X-ray | 2.6 Å | A/D=148-209 |
| 1FZF | X-ray | 2.7 Å | A/D=130-216 |
| 1RE4 | X-ray | 2.7 Å | A/D=145-210 |
| 2H43 | X-ray | 2.7 Å | A/D=130-216 |
| 2OYI | X-ray | 2.7 Å | A/D=145-210 |
Showing 20 of 39 experimental structures (best resolution first).
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