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 | 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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 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 | 0016310 | biological_process | phosphorylation |
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 | 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 | 0016310 | biological_process | phosphorylation |
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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03186 |
Chain | Residue | Details |
A | ASP229 | |
B | ASP229 | |
C | ASP229 | |
D | ASP229 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:19084537 |
Chain | Residue | Details |
A | GLY107 | |
C | ARG173 | |
C | GLY198 | |
C | SER341 | |
D | GLY107 | |
D | ARG173 | |
D | GLY198 | |
D | SER341 | |
A | ARG173 | |
A | GLY198 | |
A | SER341 | |
B | GLY107 | |
B | ARG173 | |
B | GLY198 | |
B | SER341 | |
C | GLY107 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186 |
Chain | Residue | Details |
A | ASP199 | |
B | TYR380 | |
C | ASP199 | |
C | THR227 | |
C | MET272 | |
C | GLU325 | |
C | TYR380 | |
D | ASP199 | |
D | THR227 | |
D | MET272 | |
D | GLU325 | |
A | THR227 | |
D | TYR380 | |
A | MET272 | |
A | GLU325 | |
A | TYR380 | |
B | ASP199 | |
B | THR227 | |
B | MET272 | |
B | GLU325 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19084537 |
Chain | Residue | Details |
A | LYS226 | |
B | LYS226 | |
C | LYS226 | |
D | LYS226 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
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 | |
C | GLY200 | |
D | GLY200 |