Coagulation factor X (F10) is a 488-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00742.
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The mean pLDDT of this model is 80.3 (confident 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 | 55% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting (PubMed:22409427, PubMed:39880037). Factor Xa activates pro-inflammatory signaling pathways in a protease-activated receptor (PAR)-dependent manner (PubMed:24041930, PubMed:30568593, PubMed:34831181, PubMed:18202198). Up-regulates expression of protease-activated receptors (PARs) F2R, F2RL1 and F2RL2 in dermal microvascular endothelial cells (PubMed:35738824). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, in cardiac fibroblasts and umbilical vein endothelial cells in PAR-1/F2R-dependent manner…
The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5. Interacts (inactive and activated) with ixolaris, an anticoagulant protein from Ixodes scapularis saliva (PubMed:11986214, PubMed:31133602, PubMed:18042685, PubMed:16807644). Interacts (activated) with iripin-8, a…
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9I24 | X-ray | 1.2 Å | H=235-486, L=126-179 |
| 2JKH | X-ray | 1.25 Å | A=235-475, L=126-180 |
| 2Y5F | X-ray | 1.29 Å | A=235-468, L=127-180 |
| 2Y5G | X-ray | 1.29 Å | A=235-468, L=127-180 |
| 2Y5H | X-ray | 1.33 Å | A=235-468, L=127-180 |
| 3KL6 | X-ray | 1.45 Å | A=235-475, B=126-179 |
| 2PR3 | X-ray | 1.5 Å | A=235-468, B=128-178 |
| 6YYX | X-ray | 1.53 Å | B=86-124 |
| 3FFG | X-ray | 1.54 Å | A=235-468, L=127-178 |
| 7YB9 | X-ray | 1.54 Å | B=86-124 |
| 4Y6D | X-ray | 1.55 Å | A=235-488, B=46-179 |
| 2VWO | X-ray | 1.6 Å | A=235-475, L=126-180 |
| 3CEN | X-ray | 1.6 Å | A=235-468, L=127-178 |
| 9FVV | X-ray | 1.6 Å | B=86-124 |
| 2VWN | X-ray | 1.61 Å | A=235-475, L=126-180 |
| 2P3U | X-ray | 1.62 Å | A=127-178, B=235-467 |
| 6Q9F | X-ray | 1.63 Å | B=86-124 |
| 2BOK | X-ray | 1.64 Å | A=235-475, L=126-180 |
| 2XBV | X-ray | 1.66 Å | A=235-475, L=126-180 |
| 7BMI | X-ray | 1.66 Å | B=86-124 |
Showing 20 of 187 experimental structures (best resolution first).
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