9DQM
Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (AMP bound)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003872 | molecular_function | 6-phosphofructokinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008443 | molecular_function | phosphofructokinase activity |
| A | 0009749 | biological_process | response to glucose |
| A | 0047334 | molecular_function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity |
| A | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008443 | molecular_function | phosphofructokinase activity |
| B | 0009749 | biological_process | response to glucose |
| B | 0047334 | molecular_function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity |
| B | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"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","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
