6QU3

Crystal Structure of Phosphofructokinase from Trypanosoma brucei in complex with an allosteric inhibitor ctcb360

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	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0020015	cellular_component	glycosome
A	0042301	molecular_function	phosphate ion binding
A	0046872	molecular_function	metal ion binding
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	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006096	biological_process	glycolytic process
B	0016301	molecular_function	kinase activity
B	0020015	cellular_component	glycosome
B	0042301	molecular_function	phosphate ion binding
B	0046872	molecular_function	metal ion binding
B	0061615	biological_process	glycolytic process through fructose-6-phosphate
C	0003872	molecular_function	6-phosphofructokinase activity
C	0005524	molecular_function	ATP binding
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	0020015	cellular_component	glycosome
C	0042301	molecular_function	phosphate ion binding
C	0046872	molecular_function	metal ion binding
C	0061615	biological_process	glycolytic process through fructose-6-phosphate
D	0003872	molecular_function	6-phosphofructokinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0016301	molecular_function	kinase activity
D	0020015	cellular_component	glycosome
D	0042301	molecular_function	phosphate ion binding
D	0046872	molecular_function	metal ion binding
D	0061615	biological_process	glycolytic process through fructose-6-phosphate

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue JJ5 A 1001

Chain	Residue
A	GLY197
A	THR431
A	VAL433
A	ARG434
D	SER23
D	HOH1133
A	GLY198
A	ASP199
A	PRO225
A	ASP231
A	LEU232
A	ARG274
A	ASP275
A	ALA430

---

site_id	AC2
Number of Residues	11
Details	binding site for residue CIT A 1002

Chain	Residue
A	CYS105
A	GLY106
A	GLY107
A	ARG173
A	GLY174
A	GLY198
A	ASP199
A	GLY200
A	THR201
A	LYS226
A	HOH1107

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 1003

Chain	Residue
A	ILE292
A	CYS293
A	ASN298
A	THR451
A	HOH1109
A	HOH1140

---

site_id	AC4
Number of Residues	5
Details	binding site for residue SEP A 1004

Chain	Residue
A	HIS236
A	ARG418
A	ARG435
A	HOH1102
D	ALA19

---

site_id	AC5
Number of Residues	11
Details	binding site for residue JJ5 B 1001

Chain	Residue
B	GLY197
B	GLY198
B	ASP199
B	ARG203
B	PRO225
B	ASP231
B	LEU232
B	ASP275
B	ALA430
B	VAL433
B	ARG434

---

site_id	AC6
Number of Residues	10
Details	binding site for residue CIT B 1002

Chain	Residue
B	CYS105
B	GLY106
B	GLY107
B	ARG173
B	GLY174
B	GLY198
B	ASP199
B	GLY200
B	THR201
B	LYS226

---

site_id	AC7
Number of Residues	5
Details	binding site for residue GOL B 1003

Chain	Residue
B	ILE292
B	CYS293
B	ASN298
B	TRP444
B	THR451

---

site_id	AC8
Number of Residues	13
Details	binding site for residue JJ5 C 1001

Chain	Residue
C	GLY197
C	GLY198
C	ASP199
C	ARG203
C	PRO225
C	THR227
C	ASP231
C	LEU232
C	ASP275
C	ALA430
C	THR431
C	VAL433
C	ARG434

---

site_id	AC9
Number of Residues	10
Details	binding site for residue CIT C 1002

Chain	Residue
C	CYS105
C	GLY106
C	GLY107
C	ARG173
C	GLY174
C	GLY198
C	ASP199
C	GLY200
C	THR201
C	LYS226

---

site_id	AD1
Number of Residues	6
Details	binding site for residue GOL C 1003

Chain	Residue
C	ILE292
C	CYS293
C	ASN298
C	TRP444
C	THR451
C	HOH1123

---

site_id	AD2
Number of Residues	13
Details	binding site for residue JJ5 D 1001

Chain	Residue
D	ASP275
D	ALA430
D	THR431
D	VAL433
D	ARG434
A	SER23
D	GLY197
D	GLY198
D	ASP199
D	ARG203
D	PRO225
D	ASP231
D	LEU232

---

site_id	AD3
Number of Residues	12
Details	binding site for residue CIT D 1002

Chain	Residue
D	CYS105
D	GLY106
D	GLY107
D	ARG173
D	GLY174
D	GLY198
D	ASP199
D	GLY200
D	THR201
D	LYS226
D	SER341
D	HOH1124

---

site_id	AD4
Number of Residues	6
Details	binding site for residue GOL D 1003

Chain	Residue
D	ILE292
D	CYS293
D	ASN298
D	LEU308
D	THR451
D	HOH1123

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03186

Chain	Residue	Details
A	ASP229
B	ASP229
C	ASP229
D	ASP229

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:19084537

Chain	Residue	Details
A	GLY107
C	ARG173
C	GLY198
C	SER341
D	GLY107
D	ARG173
D	GLY198
D	SER341
A	ARG173
A	GLY198
A	SER341
B	GLY107
B	ARG173
B	GLY198
B	SER341
C	GLY107

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186

Chain	Residue	Details
A	ASP199
B	TYR380
C	ASP199
C	THR227
C	MET272
C	GLU325
C	TYR380
D	ASP199
D	THR227
D	MET272
D	GLU325
A	THR227
D	TYR380
A	MET272
A	GLU325
A	TYR380
B	ASP199
B	THR227
B	MET272
B	GLU325

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:19084537

Chain	Residue	Details
A	LYS226
B	LYS226
C	LYS226
D	LYS226

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Important for substrate specificity; cannot use PPi as phosphoryl donor => ECO:0000255|HAMAP-Rule:MF_03186

Chain	Residue	Details
A	GLY200
B	GLY200
C	GLY200
D	GLY200

---