9MED

Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (AMP/beta-D-Glucose-6-phosphate complex)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
A	0061615	biological_process	glycolytic process through fructose-6-phosphate
B	0003872	molecular_function	6-phosphofructokinase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
B	0061615	biological_process	glycolytic process through fructose-6-phosphate
C	0003872	molecular_function	6-phosphofructokinase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006096	biological_process	glycolytic process
C	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
C	0061615	biological_process	glycolytic process through fructose-6-phosphate
D	0003872	molecular_function	6-phosphofructokinase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
D	0061615	biological_process	glycolytic process through fructose-6-phosphate

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"source":"HAMAP-Rule","id":"MF_01979","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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