Cytochrome c (CYCS) is a 105-residue protein from Equus caballus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00004.
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The mean pLDDT of this model is 98.0 (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 | 98% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain
Mitochondrion intermembrane space
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6K9J | X-ray | 0.98 Å | A=2-105 |
| 8ZXR | X-ray | 1.6 Å | B=12-22 |
| 3O1Y | X-ray | 1.75 Å | A/B/C=2-105 |
| 1WEJ | X-ray | 1.8 Å | F=2-105 |
| 3WC8 | X-ray | 1.8 Å | A=2-105 |
| 3WUI | X-ray | 1.8 Å | A=2-105 |
| 6K9I | X-ray | 1.8 Å | A=2-105 |
| 1HRC | X-ray | 1.9 Å | A=2-105 |
| 3O20 | X-ray | 1.9 Å | A/B/C=2-105 |
| 5IY5 | X-ray | 2.0 Å | 1/2=2-105 |
| 1CRC | X-ray | 2.08 Å | A/B=2-105 |
| 3NBT | X-ray | 2.1 Å | A/B/C/D/E/F=2-105 |
| 4NFG | X-ray | 2.11 Å | B=2-105 |
| 4RSZ | X-ray | 2.19 Å | A/B/C/D/E/F=2-105 |
| 3NBS | X-ray | 2.2 Å | A/B/C/D=2-105 |
| 6SUV | X-ray | 2.5 Å | AaA/BaB/CaC/DaD/EaE/FaF/GaG/HaH=2-105 |
| 1U75 | X-ray | 2.55 Å | B=2-105 |
| 2PCB | X-ray | 2.8 Å | B=2-105 |
| 3JBT | EM | 3.8 Å | B/D/F/H/J/L/N=1-105 |
| 5WVE | EM | 4.4 Å | B/D/F/H/J/L/N=1-105 |
Showing 20 of 33 experimental structures (best resolution first).
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