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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
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0020002cellular_componenthost cell plasma membrane
A0033644cellular_componenthost cell membrane
A0051289biological_processprotein homotetramerization
B0003779molecular_functionactin binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0020002cellular_componenthost cell plasma membrane
B0033644cellular_componenthost cell membrane
B0051289biological_processprotein homotetramerization
C0003779molecular_functionactin binding
C0004332molecular_functionfructose-bisphosphate aldolase activity
C0005737cellular_componentcytoplasm
C0006096biological_processglycolytic process
C0016020cellular_componentmembrane
C0016829molecular_functionlyase activity
C0020002cellular_componenthost cell plasma membrane
C0033644cellular_componenthost cell membrane
C0051289biological_processprotein homotetramerization
D0003779molecular_functionactin binding
D0004332molecular_functionfructose-bisphosphate aldolase activity
D0005737cellular_componentcytoplasm
D0006096biological_processglycolytic process
D0016020cellular_componentmembrane
D0016829molecular_functionlyase activity
D0020002cellular_componenthost cell plasma membrane
D0033644cellular_componenthost cell membrane
D0051289biological_processprotein homotetramerization
Functional Information from PROSITE/UniProt
site_idPS00158
Number of Residues11
DetailsALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. VlLEGaLLKPN
ChainResidueDetails
AVAL228-ASN238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q8I8I2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Schiff-base intermediate with dihydroxyacetone phosphate","evidences":[{"source":"UniProtKB","id":"Q8I8I2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues44
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8I8I2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00883","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ald
ChainResidueDetails
ALYS236
AASP39
AGLU194

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ald
ChainResidueDetails
BLYS236
BASP39
BGLU194

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ald
ChainResidueDetails
CLYS236
CASP39
CGLU194

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ald
ChainResidueDetails
DLYS236
DASP39
DGLU194

239803

PDB entries from 2025-08-06

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