Pyruvate kinase PKM (PKM) is a 531-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11974.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 95.8 (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 | 93% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival
Monomer and homotetramer; exists as a monomer in the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds 3,3',5-triiodo-L-thyronine (T3). Tetramer formation induces pyruvate kinase activity. The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex. FBP…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2G50 | X-ray | 1.65 Å | A/B/C/D/E/F/G/H=2-531 |
| 1A49 | X-ray | 2.1 Å | A/B/C/D/E/F/G/H=2-531 |
| 8F6M | X-ray | 2.15 Å | A/B/C/D/E/F/G/H=1-531 |
| 7R6Y | X-ray | 2.25 Å | A/B/C/D=1-531 |
| 8F5U | X-ray | 2.3 Å | A/B/C/D=1-531 |
| 1A5U | X-ray | 2.35 Å | A/B/C/D/E/F/G/H=2-531 |
| 3N25 | X-ray | 2.41 Å | A/B/C/D/E/F/G/H=1-531 |
| 8F5T | X-ray | 2.41 Å | A/B/C/D/E/F/G/H=1-531 |
| 1AQF | X-ray | 2.7 Å | A/B/C/D/E/F/G/H=2-531 |
| 1F3X | X-ray | 2.8 Å | A/B/C/D/E/F/G/H=2-531 |
| 1PKN | X-ray | 2.9 Å | A=2-531 |
| 1F3W | X-ray | 3.0 Å | A/B/C/D/E/F/G/H=2-531 |
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