4TR9
Ternary co-crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP and a small molecule inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003779 | molecular_function | actin binding |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008154 | biological_process | actin polymerization or depolymerization |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0003779 | molecular_function | actin binding |
| B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008154 | biological_process | actin polymerization or depolymerization |
| B | 0016020 | cellular_component | membrane |
| B | 0016829 | molecular_function | lyase activity |
| B | 0020002 | cellular_component | host cell plasma membrane |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0003779 | molecular_function | actin binding |
| C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006096 | biological_process | glycolytic process |
| C | 0008154 | biological_process | actin polymerization or depolymerization |
| C | 0016020 | cellular_component | membrane |
| C | 0016829 | molecular_function | lyase activity |
| C | 0020002 | cellular_component | host cell plasma membrane |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0003779 | molecular_function | actin binding |
| D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006096 | biological_process | glycolytic process |
| D | 0008154 | biological_process | actin polymerization or depolymerization |
| D | 0016020 | cellular_component | membrane |
| D | 0016829 | molecular_function | lyase activity |
| D | 0020002 | cellular_component | host cell plasma membrane |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue 38D A 401 |
| Chain | Residue |
| A | ASP39 |
| A | HOH618 |
| H | ASP604 |
| H | ASN606 |
| A | THR44 |
| A | LYS151 |
| A | ARG153 |
| A | GLU194 |
| A | LYS236 |
| A | HOH525 |
| A | HOH527 |
| A | HOH564 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue 38D B 401 |
| Chain | Residue |
| B | ASP39 |
| B | SER41 |
| B | THR44 |
| B | LYS47 |
| B | LYS112 |
| B | LYS151 |
| B | ARG153 |
| B | HOH502 |
| B | HOH569 |
| B | HOH594 |
| I | ASP604 |
| I | ASN606 |
| I | HOH702 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue 38D C 401 |
| Chain | Residue |
| C | ASP39 |
| C | THR44 |
| C | LYS47 |
| C | LYS112 |
| C | LYS151 |
| C | HOH510 |
| C | HOH533 |
| C | HOH555 |
| C | HOH560 |
| C | HOH574 |
| C | HOH599 |
| C | HOH614 |
| J | ASN606 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue 38D K 701 |
| Chain | Residue |
| D | ASP39 |
| D | THR44 |
| D | ARG48 |
| D | LYS112 |
| D | LYS151 |
| D | ARG153 |
| K | ASP604 |
| K | TRP605 |
| K | ASN606 |
| K | HOH801 |
Functional Information from PROSITE/UniProt
| site_id | PS00158 |
| Number of Residues | 11 |
| Details | ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. VlLEGaLLKPN |
| Chain | Residue | Details |
| A | VAL228-ASN238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00883 |
| Chain | Residue | Details |
| A | GLU194 | |
| B | GLU194 | |
| C | GLU194 | |
| D | GLU194 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Schiff-base intermediate with dihydroxyacetone-P => ECO:0000250|UniProtKB:P00883 |
| Chain | Residue | Details |
| A | LYS236 | |
| B | LYS236 | |
| C | LYS236 | |
| D | LYS236 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00883 |
| Chain | Residue | Details |
| C | SER278 | |
| C | SER306 | |
| C | ARG309 | |
| D | ARG48 | |
| D | SER278 | |
| D | SER306 | |
| D | ARG309 | |
| C | ARG48 | |
| A | ARG48 | |
| A | SER278 | |
| A | SER306 | |
| A | ARG309 | |
| B | ARG48 | |
| B | SER278 | |
| B | SER306 | |
| B | ARG309 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate => ECO:0000250|UniProtKB:P00883 |
| Chain | Residue | Details |
| A | TYR368 | |
| B | TYR368 | |
| C | TYR368 | |
| D | TYR368 |
