9DQM
Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (AMP bound)
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01979 |
| Chain | Residue | Details |
| A | ASP142 | |
| B | ASP142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01979 |
| Chain | Residue | Details |
| A | GLY15 | |
| B | MET186 | |
| B | GLU247 | |
| B | TYR308 | |
| A | ASP114 | |
| A | THR140 | |
| A | MET186 | |
| A | GLU247 | |
| A | TYR308 | |
| B | GLY15 | |
| B | ASP114 | |
| B | THR140 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP => ECO:0000255|HAMAP-Rule:MF_01979 |
| Chain | Residue | Details |
| A | ASP115 | |
| B | ASP115 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi => ECO:0000255|HAMAP-Rule:MF_01979 |
| Chain | Residue | Details |
| A | LYS139 | |
| B | LYS139 |
