6QU3
Crystal Structure of Phosphofructokinase from Trypanosoma brucei in complex with an allosteric inhibitor ctcb360
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0016740 | molecular_function | transferase 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 0016740 | molecular_function | transferase 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003872 | molecular_function | 6-phosphofructokinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0020015 | cellular_component | glycosome |
| C | 0042301 | molecular_function | phosphate ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003872 | molecular_function | 6-phosphofructokinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0020015 | cellular_component | glycosome |
| D | 0042301 | molecular_function | phosphate ion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue JJ5 A 1001 |
| Chain | Residue |
| A | GLY197 |
| A | THR431 |
| A | VAL433 |
| A | ARG434 |
| D | SER23 |
| D | HOH1133 |
| A | GLY198 |
| A | ASP199 |
| A | PRO225 |
| A | ASP231 |
| A | LEU232 |
| A | ARG274 |
| A | ASP275 |
| A | ALA430 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue CIT A 1002 |
| Chain | Residue |
| A | CYS105 |
| A | GLY106 |
| A | GLY107 |
| A | ARG173 |
| A | GLY174 |
| A | GLY198 |
| A | ASP199 |
| A | GLY200 |
| A | THR201 |
| A | LYS226 |
| A | HOH1107 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 1003 |
| Chain | Residue |
| A | ILE292 |
| A | CYS293 |
| A | ASN298 |
| A | THR451 |
| A | HOH1109 |
| A | HOH1140 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SEP A 1004 |
| Chain | Residue |
| A | HIS236 |
| A | ARG418 |
| A | ARG435 |
| A | HOH1102 |
| D | ALA19 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue JJ5 B 1001 |
| Chain | Residue |
| B | GLY197 |
| B | GLY198 |
| B | ASP199 |
| B | ARG203 |
| B | PRO225 |
| B | ASP231 |
| B | LEU232 |
| B | ASP275 |
| B | ALA430 |
| B | VAL433 |
| B | ARG434 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue CIT B 1002 |
| Chain | Residue |
| B | CYS105 |
| B | GLY106 |
| B | GLY107 |
| B | ARG173 |
| B | GLY174 |
| B | GLY198 |
| B | ASP199 |
| B | GLY200 |
| B | THR201 |
| B | LYS226 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 1003 |
| Chain | Residue |
| B | ILE292 |
| B | CYS293 |
| B | ASN298 |
| B | TRP444 |
| B | THR451 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue JJ5 C 1001 |
| Chain | Residue |
| C | GLY197 |
| C | GLY198 |
| C | ASP199 |
| C | ARG203 |
| C | PRO225 |
| C | THR227 |
| C | ASP231 |
| C | LEU232 |
| C | ASP275 |
| C | ALA430 |
| C | THR431 |
| C | VAL433 |
| C | ARG434 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue CIT C 1002 |
| Chain | Residue |
| C | CYS105 |
| C | GLY106 |
| C | GLY107 |
| C | ARG173 |
| C | GLY174 |
| C | GLY198 |
| C | ASP199 |
| C | GLY200 |
| C | THR201 |
| C | LYS226 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 1003 |
| Chain | Residue |
| C | ILE292 |
| C | CYS293 |
| C | ASN298 |
| C | TRP444 |
| C | THR451 |
| C | HOH1123 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for residue JJ5 D 1001 |
| Chain | Residue |
| D | ASP275 |
| D | ALA430 |
| D | THR431 |
| D | VAL433 |
| D | ARG434 |
| A | SER23 |
| D | GLY197 |
| D | GLY198 |
| D | ASP199 |
| D | ARG203 |
| D | PRO225 |
| D | ASP231 |
| D | LEU232 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue CIT D 1002 |
| Chain | Residue |
| D | CYS105 |
| D | GLY106 |
| D | GLY107 |
| D | ARG173 |
| D | GLY174 |
| D | GLY198 |
| D | ASP199 |
| D | GLY200 |
| D | THR201 |
| D | LYS226 |
| D | SER341 |
| D | HOH1124 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 1003 |
| Chain | Residue |
| D | ILE292 |
| D | CYS293 |
| D | ASN298 |
| D | LEU308 |
| D | THR451 |
| D | HOH1123 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19084537","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19084537","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for substrate specificity; cannot use PPi as phosphoryl donor","evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
