6SY7
Structure of Trypanosome Brucei Phosphofructokinase in complex with AMP.
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 |
| 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 | 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 | 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 |
| E | 0003872 | molecular_function | 6-phosphofructokinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| E | 0006096 | biological_process | glycolytic process |
| E | 0016301 | molecular_function | kinase activity |
| E | 0020015 | cellular_component | glycosome |
| E | 0042301 | molecular_function | phosphate ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| F | 0003872 | molecular_function | 6-phosphofructokinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| F | 0006096 | biological_process | glycolytic process |
| F | 0016301 | molecular_function | kinase activity |
| F | 0020015 | cellular_component | glycosome |
| F | 0042301 | molecular_function | phosphate ion binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| G | 0003872 | molecular_function | 6-phosphofructokinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| G | 0006096 | biological_process | glycolytic process |
| G | 0016301 | molecular_function | kinase activity |
| G | 0020015 | cellular_component | glycosome |
| G | 0042301 | molecular_function | phosphate ion binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| H | 0003872 | molecular_function | 6-phosphofructokinase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| H | 0006096 | biological_process | glycolytic process |
| H | 0016301 | molecular_function | kinase activity |
| H | 0020015 | cellular_component | glycosome |
| H | 0042301 | molecular_function | phosphate ion binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue BNZ A 501 |
| Chain | Residue |
| A | GLY198 |
| A | ASP199 |
| A | LEU232 |
| A | HOH697 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ILE292 |
| A | CYS293 |
| A | ASN298 |
| A | THR451 |
| A | HOH618 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue AMP A 503 |
| Chain | Residue |
| A | ALA288 |
| A | GLN289 |
| A | ALA290 |
| A | ASN291 |
| A | ARG312 |
| A | ILE450 |
| A | HOH619 |
| A | HOH647 |
| B | ARG117 |
| B | SER118 |
| B | LEU121 |
| B | THR122 |
| B | ASN125 |
| B | ARG155 |
| B | THR400 |
| B | HOH1144 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue AMP B 1001 |
| Chain | Residue |
| A | ARG117 |
| A | SER118 |
| A | LEU121 |
| A | THR122 |
| A | ASN125 |
| A | ARG155 |
| A | THR400 |
| B | ALA288 |
| B | GLN289 |
| B | ALA290 |
| B | ASN291 |
| B | ARG312 |
| B | ILE450 |
| B | HOH1116 |
| B | HOH1129 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue BNZ B 1002 |
| Chain | Residue |
| B | GLY198 |
| B | ASP199 |
| B | LEU232 |
| B | ALA430 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 1003 |
| Chain | Residue |
| B | ILE292 |
| B | CYS293 |
| B | ASN298 |
| B | THR451 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue BNZ C 501 |
| Chain | Residue |
| C | GLY198 |
| C | ASP199 |
| C | LEU232 |
| C | ALA430 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | ILE292 |
| C | CYS293 |
| C | ASN298 |
| C | TRP444 |
| C | THR451 |
| C | HOH635 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue AMP C 503 |
| Chain | Residue |
| C | ALA288 |
| C | GLN289 |
| C | ALA290 |
| C | ASN291 |
| C | ARG312 |
| C | ILE450 |
| C | HOH617 |
| D | ARG117 |
| D | SER118 |
| D | LEU121 |
| D | THR122 |
| D | ASN125 |
| D | ARG155 |
| D | THR400 |
| D | HOH1117 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue AMP D 1001 |
| Chain | Residue |
| C | ARG117 |
| C | SER118 |
| C | LEU121 |
| C | THR122 |
| C | ASN125 |
| C | ARG155 |
| C | THR400 |
| D | ALA288 |
| D | GLN289 |
| D | ALA290 |
| D | ASN291 |
| D | ARG312 |
| D | ILE450 |
| D | HOH1107 |
| D | HOH1112 |
| D | HOH1131 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue BNZ D 1002 |
| Chain | Residue |
| D | GLY198 |
| D | ASP199 |
| D | ASP231 |
| D | LEU232 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 1003 |
| Chain | Residue |
| D | HOH1102 |
| D | ILE292 |
| D | CYS293 |
| D | LEU294 |
| D | ASN298 |
| D | TRP444 |
| D | THR451 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue BNZ E 501 |
| Chain | Residue |
| E | GLY198 |
| E | ASP199 |
| E | LEU232 |
| E | ALA430 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL E 502 |
| Chain | Residue |
| E | ILE292 |
| E | CYS293 |
| E | ASN298 |
| E | THR451 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for residue AMP F 1001 |
| Chain | Residue |
| E | ARG117 |
| E | SER118 |
| E | LEU121 |
| E | THR122 |
| E | ASN125 |
| E | ARG155 |
| E | THR400 |
| F | ALA288 |
| F | GLN289 |
| F | ALA290 |
| F | ASN291 |
| F | ARG312 |
| F | ILE450 |
| F | HOH1102 |
| F | HOH1105 |
| site_id | AD7 |
| Number of Residues | 15 |
| Details | binding site for residue AMP F 1002 |
| Chain | Residue |
| E | ALA288 |
| E | GLN289 |
| E | ALA290 |
| E | ASN291 |
| E | ARG312 |
| E | ILE450 |
| E | HOH612 |
| E | HOH627 |
| F | ARG117 |
| F | SER118 |
| F | LEU121 |
| F | THR122 |
| F | ASN125 |
| F | ARG155 |
| F | THR400 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue BNZ F 1003 |
| Chain | Residue |
| F | GLY198 |
| F | ASP199 |
| F | LEU232 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL F 1004 |
| Chain | Residue |
| F | ILE292 |
| F | CYS293 |
| F | ASN298 |
| F | THR451 |
| F | HOH1117 |
| F | HOH1132 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue BNZ G 501 |
| Chain | Residue |
| G | GLY198 |
| G | ASP199 |
| G | LEU232 |
| G | ALA430 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL G 502 |
| Chain | Residue |
| G | ILE292 |
| G | CYS293 |
| G | LEU294 |
| G | ASN298 |
| G | THR451 |
| G | HOH601 |
| G | HOH616 |
| site_id | AE3 |
| Number of Residues | 14 |
| Details | binding site for residue AMP G 503 |
| Chain | Residue |
| G | ALA288 |
| G | GLN289 |
| G | ALA290 |
| G | ASN291 |
| G | ARG312 |
| G | ILE450 |
| H | ARG117 |
| H | SER118 |
| H | LEU121 |
| H | THR122 |
| H | ASN125 |
| H | ARG155 |
| H | THR400 |
| H | HOH1124 |
| site_id | AE4 |
| Number of Residues | 15 |
| Details | binding site for residue AMP H 1001 |
| Chain | Residue |
| G | ARG117 |
| G | SER118 |
| G | LEU121 |
| G | THR122 |
| G | ASN125 |
| G | ARG155 |
| G | THR400 |
| H | ALA288 |
| H | GLN289 |
| H | ALA290 |
| H | ASN291 |
| H | ARG312 |
| H | ILE450 |
| H | HOH1111 |
| H | HOH1114 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue BNZ H 1002 |
| Chain | Residue |
| H | GLY198 |
| H | ASP199 |
| H | LEU232 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL H 1003 |
| Chain | Residue |
| H | ASN291 |
| H | CYS293 |
| H | ASN298 |
| H | THR451 |
| H | VAL452 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03186 |
| Chain | Residue | Details |
| A | ASP229 | |
| B | ASP229 | |
| C | ASP229 | |
| D | ASP229 | |
| E | ASP229 | |
| F | ASP229 | |
| G | ASP229 | |
| H | ASP229 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| 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 | |
| E | GLY107 | |
| E | ARG173 | |
| E | GLY198 | |
| A | ARG173 | |
| E | SER341 | |
| F | GLY107 | |
| F | ARG173 | |
| F | GLY198 | |
| F | SER341 | |
| G | GLY107 | |
| G | ARG173 | |
| G | GLY198 | |
| G | SER341 | |
| H | GLY107 | |
| A | GLY198 | |
| H | ARG173 | |
| H | GLY198 | |
| H | SER341 | |
| A | SER341 | |
| B | GLY107 | |
| B | ARG173 | |
| B | GLY198 | |
| B | SER341 | |
| C | GLY107 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| 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 | |
| E | ASP199 | |
| E | THR227 | |
| E | MET272 | |
| E | GLU325 | |
| E | TYR380 | |
| F | ASP199 | |
| F | THR227 | |
| F | MET272 | |
| F | GLU325 | |
| A | MET272 | |
| F | TYR380 | |
| G | ASP199 | |
| G | THR227 | |
| G | MET272 | |
| G | GLU325 | |
| G | TYR380 | |
| H | ASP199 | |
| H | THR227 | |
| H | MET272 | |
| H | GLU325 | |
| A | GLU325 | |
| H | TYR380 | |
| A | TYR380 | |
| B | ASP199 | |
| B | THR227 | |
| B | MET272 | |
| B | GLU325 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19084537 |
| Chain | Residue | Details |
| A | LYS226 | |
| B | LYS226 | |
| C | LYS226 | |
| D | LYS226 | |
| E | LYS226 | |
| F | LYS226 | |
| G | LYS226 | |
| H | LYS226 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| 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 | |
| E | GLY200 | |
| F | GLY200 | |
| G | GLY200 | |
| H | GLY200 |
