2PC4
Crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP-tail determined at 2.4 angstrom resolution
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 | 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 | 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 | 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 | 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 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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q8I8I2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Schiff-base intermediate with dihydroxyacetone phosphate","evidences":[{"source":"UniProtKB","id":"Q8I8I2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8I8I2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| A | LYS236 | |
| A | ASP39 | |
| A | GLU194 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| B | LYS236 | |
| B | ASP39 | |
| B | GLU194 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| C | LYS236 | |
| C | ASP39 | |
| C | GLU194 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| D | LYS236 | |
| D | ASP39 | |
| D | GLU194 |
