2HIG
Crystal Structure of Phosphofructokinase apoenzyme from Trypanosoma brucei.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003872 | molecular_function | 6-phosphofructokinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0020015 | cellular_component | glycosome |
| A | 0042301 | molecular_function | phosphate ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0020015 | cellular_component | glycosome |
| B | 0042301 | molecular_function | phosphate ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 488 |
| Chain | Residue |
| A | ALA259 |
| A | VAL260 |
| A | ALA262 |
| A | ARG317 |
| A | SER318 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 488 |
| Chain | Residue |
| B | SER318 |
| B | HOH532 |
| B | ALA259 |
| B | VAL260 |
| B | ALA262 |
| B | ARG317 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03186 |
| Chain | Residue | Details |
| A | ASP229 | |
| B | ASP229 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:19084537 |
| Chain | Residue | Details |
| A | GLY198 | |
| A | SER341 | |
| B | GLY107 | |
| B | ARG173 | |
| B | GLY198 | |
| B | SER341 | |
| A | GLY107 | |
| A | ARG173 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186 |
| Chain | Residue | Details |
| A | MET272 | |
| A | GLU325 | |
| A | TYR380 | |
| B | ASP199 | |
| B | THR227 | |
| B | MET272 | |
| B | GLU325 | |
| B | TYR380 | |
| A | ASP199 | |
| A | THR227 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19084537 |
| Chain | Residue | Details |
| A | LYS226 | |
| B | LYS226 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Important for substrate specificity; cannot use PPi as phosphoryl donor => ECO:0000255|HAMAP-Rule:MF_03186 |
| Chain | Residue | Details |
| A | GLY200 | |
| B | GLY200 |
