Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6QU5

Crystal Structure of Phosphofructokinase from Trypanosoma brucei in complex with an allosteric inhibitor ctcb12

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
E	0003872	molecular_function	6-phosphofructokinase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006002	biological_process	fructose 6-phosphate metabolic process
E	0006096	biological_process	glycolytic process
E	0016301	molecular_function	kinase activity
E	0020015	cellular_component	glycosome
E	0042301	molecular_function	phosphate ion binding
E	0046872	molecular_function	metal ion binding
E	0061615	biological_process	glycolytic process through fructose-6-phosphate
F	0003872	molecular_function	6-phosphofructokinase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006002	biological_process	fructose 6-phosphate metabolic process
F	0006096	biological_process	glycolytic process
F	0016301	molecular_function	kinase activity
F	0020015	cellular_component	glycosome
F	0042301	molecular_function	phosphate ion binding
F	0046872	molecular_function	metal ion binding
F	0061615	biological_process	glycolytic process through fructose-6-phosphate
G	0003872	molecular_function	6-phosphofructokinase activity
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006002	biological_process	fructose 6-phosphate metabolic process
G	0006096	biological_process	glycolytic process
G	0016301	molecular_function	kinase activity
G	0020015	cellular_component	glycosome
G	0042301	molecular_function	phosphate ion binding
G	0046872	molecular_function	metal ion binding
G	0061615	biological_process	glycolytic process through fructose-6-phosphate
H	0003872	molecular_function	6-phosphofructokinase activity
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0006002	biological_process	fructose 6-phosphate metabolic process
H	0006096	biological_process	glycolytic process
H	0016301	molecular_function	kinase activity
H	0020015	cellular_component	glycosome
H	0042301	molecular_function	phosphate ion binding
H	0046872	molecular_function	metal ion binding
H	0061615	biological_process	glycolytic process through fructose-6-phosphate

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue CIT A 501

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

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 502

Chain	Residue
A	ILE292
A	CYS293
A	ASN298
A	TRP444
A	THR451
A	VAL452

site_id	AC3
Number of Residues	8
Details	binding site for residue JJ8 A 503

Chain	Residue
A	HIS17
A	GLY197
A	GLY198
A	ASP199
A	LEU232
A	ASP275
A	ALA430
A	ARG434

site_id	AC4
Number of Residues	10
Details	binding site for residue CIT B 501

Chain	Residue
B	GLY106
B	GLY107
B	ARG173
B	GLY198
B	ASP199
B	GLY200
B	THR201
B	LYS226
B	SER341
B	ASN343

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL B 502

Chain	Residue
B	ILE292
B	CYS293
B	ASN298
B	ARG448
B	THR451

site_id	AC6
Number of Residues	11
Details	binding site for residue JJ8 B 503

Chain	Residue
B	GLY197
B	GLY198
B	ASP199
B	GLN202
B	PRO225
B	ASP231
B	LEU232
B	ASP275
B	ALA430
B	VAL433
B	ARG434

site_id	AC7
Number of Residues	9
Details	binding site for residue CIT C 501

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

site_id	AC8
Number of Residues	9
Details	binding site for residue CIT D 501

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

site_id	AC9
Number of Residues	8
Details	binding site for residue CIT E 501

Chain	Residue
E	GLY106
E	ARG173
E	GLY174
E	GLY198
E	ASP199
E	GLY200
E	THR201
E	LYS226

site_id	AD1
Number of Residues	8
Details	binding site for residue CIT F 501

Chain	Residue
F	GLY106
F	GLY107
F	ARG173
F	GLY198
F	ASP199
F	GLY200
F	THR201
F	LYS226

site_id	AD2
Number of Residues	8
Details	binding site for residue CIT G 501

Chain	Residue
G	GLY106
G	ARG173
G	GLY174
G	GLY198
G	ASP199
G	GLY200
G	THR201
G	LYS226

site_id	AD3
Number of Residues	8
Details	binding site for Di-peptide CIT H 501 and ARG H 173

Chain	Residue
H	GLY107
H	SER172
H	GLY174
H	GLY198
H	ASP199
H	GLY200
H	THR201
H	LYS226

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_03186

Chain	Residue	Details
A	ASP229
B	ASP229
C	ASP229
D	ASP229
E	ASP229
F	ASP229
G	ASP229
H	ASP229

site_id	SWS_FT_FI2
Number of Residues	32
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
E	GLY107
E	ARG173
E	GLY198
A	ARG173
E	SER341
F	GLY107
F	ARG173
F	GLY198
F	SER341
G	GLY107
G	ARG173
G	GLY198
G	SER341
H	GLY107
A	GLY198
H	ARG173
H	GLY198
H	SER341
A	SER341
B	GLY107
B	ARG173
B	GLY198
B	SER341
C	GLY107

site_id	SWS_FT_FI3
Number of Residues	40
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
E	ASP199
E	THR227
E	MET272
E	GLU325
E	TYR380
F	ASP199
F	THR227
F	MET272
F	GLU325
A	MET272
F	TYR380
G	ASP199
G	THR227
G	MET272
G	GLU325
G	TYR380
H	ASP199
H	THR227
H	MET272
H	GLU325
A	GLU325
H	TYR380
A	TYR380
B	ASP199
B	THR227
B	MET272
B	GLU325

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:19084537

Chain	Residue	Details
A	LYS226
B	LYS226
C	LYS226
D	LYS226
E	LYS226
F	LYS226
G	LYS226
H	LYS226

site_id	SWS_FT_FI5
Number of Residues	8
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
E	GLY200
F	GLY200
G	GLY200
H	GLY200

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)