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
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
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
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

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

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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

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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

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site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00883

Chain	Residue	Details
A	ARG48
C	SER278
C	SER306
C	ARG309
D	ARG48
D	SER278
D	SER306
D	ARG309
A	SER278
A	SER306
A	ARG309
B	ARG48
B	SER278
B	SER306
B	ARG309
C	ARG48

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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

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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

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ald

Chain	Residue	Details
B	LYS236
B	ASP39
B	GLU194

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ald

Chain	Residue	Details
C	LYS236
C	ASP39
C	GLU194

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site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ald

Chain	Residue	Details
D	LYS236
D	ASP39
D	GLU194

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