Complement factor H (CFH) is a 1231-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08603.
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The mean pLDDT of this model is 78.3 (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 | 1% |
| 70 to 90 | Confident: backbone generally right | 85% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces (PubMed:21285368, PubMed:21317894, PubMed:25402769). Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop (PubMed:19503104, PubMed:21317894, PubMed:26700768). As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited…
Homodimer (PubMed:18005991, PubMed:19505476). Also forms homooligomers (PubMed:19505476). Interacts with complement protein C3b; this interaction inhibits complement activation (PubMed:16601698, PubMed:19503104, PubMed:20378178, PubMed:21285368, PubMed:28671664). Interacts with complement protein C3d (PubMed:20378178, PubMed:21285368, PubMed:29190743). Interacts with CR3/ITGAM; this interaction…
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4K12 | X-ray | 1.08 Å | A=508-567 |
| 3R62 | X-ray | 1.52 Å | A/B=1107-1231 |
| 3KZJ | X-ray | 1.65 Å | A=1103-1231 |
| 2G7I | X-ray | 1.75 Å | A=1107-1231 |
| 3SW0 | X-ray | 1.8 Å | X=1046-1231 |
| 6ATG | X-ray | 1.8 Å | A/D=388-446 |
| 9MLU | X-ray | 1.82 Å | A/B=321-443 |
| 9MMX | X-ray | 1.9 Å | A/B=321-443 |
| 3KXV | X-ray | 2.0 Å | A=1103-1231 |
| 3OXU | X-ray | 2.1 Å | D/E/F=1107-1231 |
| 4ONT | X-ray | 2.15 Å | D/E/F=1107-1231 |
| 6ZH1 | X-ray | 2.2 Å | B=1104-1231 |
| 4ZH1 | X-ray | 2.24 Å | D/E/F=1107-1231 |
| 9MMU | X-ray | 2.25 Å | C/D/G/H=321-443 |
| 2XQW | X-ray | 2.31 Å | C=1103-1231 |
| 4AYI | X-ray | 2.31 Å | A/E=321-443 |
| 2UWN | X-ray | 2.35 Å | A=322-506 |
| 2W80 | X-ray | 2.35 Å | A/B/E/G=321-443 |
| 2W81 | X-ray | 2.35 Å | A/B/E=321-443 |
| 3RJ3 | X-ray | 2.35 Å | D/E/F=1107-1231 |
Showing 20 of 51 experimental structures (best resolution first).
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