Table 1. Comparison of human PFK-M, PFK-L and PFK-P sequences shows weak conservation at Interface 2 residues compared with Interface 1 residues.
| PFK-M | PFK-L | PFK-P | |||
|---|---|---|---|---|---|
| PFK-M | Overall identity | - | 69% | 68% | |
| - | 780 AA | Interface1 | - | 88% (58/66) | 91% (60/66) |
| - | 85.18 kDa | Interface 2 | - | 63% (12/19) | 79% (15/19) |
| ATP site | - | 88% (7/8) | 100% (8/8) | ||
| F26BP site | 84% (16/19) | 95% (18/19) | |||
| Allosteric site A | - | 87% (13/15) | 80% (12/15) | ||
| Allosteric site B | - | 88% (15/17) | 82% (14/17) | ||
| PFK-L | Overall identity | 69% | - | 71% | |
| - | 780 AA | Interface1 | 88% (58/66) | - | 89% (59/66) |
| - | 85.02 kDa | Interface 2 | 63% (12/19) | - | 58% (11/19) |
| ATP site | 88% (7/8) | - | 88% (7/8) | ||
| F26BP site | 84% (16/19) | - | 84% (16/19) | ||
| Allosteric site A | 87% (13/15) | - | 67% (10/15) | ||
| Allosteric site B | 76% (13/17) | - | 82% (14/17) | ||
| PFK-P | Overall identity | 68% | 71% | - | |
| - | 784 AA | Interface1 | 91% (60/66) | 89% (59/66) | - |
| - | 85.60 kDa | Interface 2 | 79% (15/19) | 58% (11/19) | - |
| ATP site | 100% (8/8) | 88% (8/8) | - | ||
| F26BP site | 95% (18/19) | 84% (16/19) | - | ||
| Allosteric site A | 80% (12/15) | 67% (10/15) | - | ||
| Allosteric site B | 82% (14/17) | 88% (15/17) | - |
Residues involved in Interface 1, Interface 2, and binding pockets for ATP and F26BP (Figure 1) were identified using PDBePISA1 using the PFK-P structure (PDB 4XYJ). Allosteric sites A and B (Figure 1) were identified by overlying the structure of EcPFK complex with ADP (PDB PFK1). Supplementary Table S2 compares Interface 1 amino acid sequences; Supplementary Table S3 compares Interface 2 amino acid sequences.