3K2Q

Crystal structure of Pyrophosphate-dependent phosphofructokinase from Marinobacter aquaeolei, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MqR88

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005737	cellular_component	cytoplasm
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
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	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
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	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006096	biological_process	glycolytic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0046835	biological_process	carbohydrate phosphorylation
C	0046872	molecular_function	metal ion binding
C	0047334	molecular_function	diphosphate-fructose-6-phosphate 1-phosphotransferase activity
C	0061615	biological_process	glycolytic process through fructose-6-phosphate

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA A 421

Chain	Residue
A	ARG80
A	HOH438

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA B 421

Chain	Residue
B	ARG80

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA C 421

Chain	Residue
C	ARG80
C	HOH526

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
A	THR142
A	GLY13
A	ARG80
A	ARG192
A	ASP144

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site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
B	THR142
B	GLY13
B	ARG80
B	ARG192
B	ASP144

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site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
C	THR142
C	GLY13
C	ARG80
C	ARG192
C	ASP144

---

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
A	GLY13
A	THR142
A	ARG80
A	LYS141
A	ASP144

---

site_id	CSA5
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
B	GLY13
B	THR142
B	ARG80
B	LYS141
B	ASP144

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site_id	CSA6
Number of Residues	5
Details	Annotated By Reference To The Literature 1pfk

Chain	Residue	Details
C	GLY13
C	THR142
C	ARG80
C	LYS141
C	ASP144

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