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2EPH

Crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP-tail determined at 2.7 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0020002cellular_componenthost cell plasma membrane
A0030388biological_processfructose 1,6-bisphosphate metabolic process
B0003779molecular_functionactin binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0020002cellular_componenthost cell plasma membrane
B0030388biological_processfructose 1,6-bisphosphate metabolic process
C0003779molecular_functionactin binding
C0004332molecular_functionfructose-bisphosphate aldolase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0016020cellular_componentmembrane
C0016829molecular_functionlyase activity
C0020002cellular_componenthost cell plasma membrane
C0030388biological_processfructose 1,6-bisphosphate metabolic process
D0003779molecular_functionactin binding
D0004332molecular_functionfructose-bisphosphate aldolase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0016020cellular_componentmembrane
D0016829molecular_functionlyase activity
D0020002cellular_componenthost cell plasma membrane
D0030388biological_processfructose 1,6-bisphosphate metabolic process
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
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q8I8I2
ChainResidueDetails
AGLU194
BGLU194
CGLU194
DGLU194

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with dihydroxyacetone phosphate => ECO:0000250|UniProtKB:Q8I8I2
ChainResidueDetails
ALYS236
BLYS236
CLYS236
DLYS236

site_idSWS_FT_FI3
Number of Residues44
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8I8I2
ChainResidueDetails
AASP39
AGLY308
AARG309
BASP39
BSER41
BTHR44
BLYS112
BLYS151
BGLU194
BLYS236
BSER278
ASER41
BGLY279
BGLY308
BARG309
CASP39
CSER41
CTHR44
CLYS112
CLYS151
CGLU194
CLYS236
ATHR44
CSER278
CGLY279
CGLY308
CARG309
DASP39
DSER41
DTHR44
DLYS112
DLYS151
DGLU194
ALYS112
DLYS236
DSER278
DGLY279
DGLY308
DARG309
ALYS151
AGLU194
ALYS236
ASER278
AGLY279

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
AARG48
ASER306
BARG48
BSER306
CARG48
CSER306
DARG48
DSER306

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
ATYR368
BTYR368
CTYR368
DTYR368

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

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PDB entries from 2024-10-30

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