1KZH

Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005524	molecular_function	ATP binding
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	0008443	molecular_function	phosphofructokinase activity
A	0009749	biological_process	response to glucose
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
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	0005524	molecular_function	ATP binding
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	0008443	molecular_function	phosphofructokinase activity
B	0009749	biological_process	response to glucose
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 600

Chain	Residue
A	GLY82
A	ARG146
A	ARG431
B	THR241
B	LYS243
B	TYR244

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 601

Chain	Residue
A	ASP177
A	SER178
A	LYS203
A	HOH794
A	HOH801
A	ARG146
A	GLY175
A	ASP176

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 602

Chain	Residue
A	LYS71
A	ALA72
A	ASN102
A	ASN104

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1600

Chain	Residue
A	THR241
A	LYS243
A	TYR244
B	ARG146
B	ARG431

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1601

Chain	Residue
B	SER80
B	GLY81
B	ARG146
B	GLY175
B	ASP177
B	SER178
B	LYS203

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1602

Chain	Residue
B	LYS71
B	ALA72
B	ASN102
B	ASN104

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 1603

Chain	Residue
A	HIS424
A	PHE425
A	HOH759
A	HOH783
B	HIS424
B	PHE425

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1604

Chain	Residue
B	LYS23
B	ASP24
B	ASN27
B	GLU62

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980

Chain	Residue	Details
A	ASP206
B	ASP206

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5

Chain	Residue	Details
A	GLY82
A	LYS243
B	GLY82
B	LYS243

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269|Ref.5

Chain	Residue	Details
A	ARG146
B	ARG146

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980

Chain	Residue	Details
A	ASP176
B	ASP176

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5

Chain	Residue	Details
A	THR204
A	MET251
A	GLU312
A	TYR428
B	THR204
B	MET251
B	GLU312
B	TYR428

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: 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 => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149

Chain	Residue	Details
A	ASP177
B	ASP177

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149

Chain	Residue	Details
A	LYS203
B	LYS203

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 12015149

Chain	Residue	Details
A	THR204
A	ASP206
A	GLY82
A	LYS203
A	ARG146

---

site_id	CSA2
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 12015149

Chain	Residue	Details
B	THR204
B	ASP206
B	GLY82
B	LYS203
B	ARG146

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 653

Chain	Residue	Details
A	GLY82	electrostatic stabiliser, polar interaction
A	ARG146	electrostatic stabiliser, polar interaction
A	ASP177	polar interaction
A	LYS203	electrostatic stabiliser, polar interaction
A	THR204	electrostatic stabiliser, polar interaction
A	ASP206	activator, electrostatic stabiliser, polar interaction, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 653

Chain	Residue	Details
B	GLY82	electrostatic stabiliser, polar interaction
B	ARG146	electrostatic stabiliser, polar interaction
B	ASP177	polar interaction
B	LYS203	electrostatic stabiliser, polar interaction
B	THR204	electrostatic stabiliser, polar interaction
B	ASP206	activator, electrostatic stabiliser, polar interaction, proton acceptor, proton donor

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