Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7LW1

Human phosphofructokinase-1 liver type bound to activator NA-11

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005945	cellular_component	6-phosphofructokinase complex
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006096	biological_process	glycolytic process
A	0009749	biological_process	response to glucose
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019900	molecular_function	kinase binding
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0034774	cellular_component	secretory granule lumen
A	0042802	molecular_function	identical protein binding
A	0046676	biological_process	negative regulation of insulin secretion
A	0046872	molecular_function	metal ion binding
A	0048029	molecular_function	monosaccharide binding
A	0061615	biological_process	glycolytic process through fructose-6-phosphate
A	0061621	biological_process	canonical glycolysis
A	0070061	molecular_function	fructose binding
A	0070062	cellular_component	extracellular exosome
A	0070095	molecular_function	fructose-6-phosphate binding
A	1904813	cellular_component	ficolin-1-rich granule lumen
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0003872	molecular_function	6-phosphofructokinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005945	cellular_component	6-phosphofructokinase complex
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006096	biological_process	glycolytic process
D	0009749	biological_process	response to glucose
D	0016020	cellular_component	membrane
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0019900	molecular_function	kinase binding
D	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
D	0034774	cellular_component	secretory granule lumen
D	0042802	molecular_function	identical protein binding
D	0046676	biological_process	negative regulation of insulin secretion
D	0046872	molecular_function	metal ion binding
D	0048029	molecular_function	monosaccharide binding
D	0061615	biological_process	glycolytic process through fructose-6-phosphate
D	0061621	biological_process	canonical glycolysis
D	0070061	molecular_function	fructose binding
D	0070062	cellular_component	extracellular exosome
D	0070095	molecular_function	fructose-6-phosphate binding
D	1904813	cellular_component	ficolin-1-rich granule lumen
E	0000166	molecular_function	nucleotide binding
E	0003824	molecular_function	catalytic activity
E	0003872	molecular_function	6-phosphofructokinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005576	cellular_component	extracellular region
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005945	cellular_component	6-phosphofructokinase complex
E	0006002	biological_process	fructose 6-phosphate metabolic process
E	0006096	biological_process	glycolytic process
E	0009749	biological_process	response to glucose
E	0016020	cellular_component	membrane
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0019900	molecular_function	kinase binding
E	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
E	0034774	cellular_component	secretory granule lumen
E	0042802	molecular_function	identical protein binding
E	0046676	biological_process	negative regulation of insulin secretion
E	0046872	molecular_function	metal ion binding
E	0048029	molecular_function	monosaccharide binding
E	0061615	biological_process	glycolytic process through fructose-6-phosphate
E	0061621	biological_process	canonical glycolysis
E	0070061	molecular_function	fructose binding
E	0070062	cellular_component	extracellular exosome
E	0070095	molecular_function	fructose-6-phosphate binding
E	1904813	cellular_component	ficolin-1-rich granule lumen
F	0000166	molecular_function	nucleotide binding
F	0003824	molecular_function	catalytic activity
F	0003872	molecular_function	6-phosphofructokinase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005576	cellular_component	extracellular region
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005945	cellular_component	6-phosphofructokinase complex
F	0006002	biological_process	fructose 6-phosphate metabolic process
F	0006096	biological_process	glycolytic process
F	0009749	biological_process	response to glucose
F	0016020	cellular_component	membrane
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0019900	molecular_function	kinase binding
F	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
F	0034774	cellular_component	secretory granule lumen
F	0042802	molecular_function	identical protein binding
F	0046676	biological_process	negative regulation of insulin secretion
F	0046872	molecular_function	metal ion binding
F	0048029	molecular_function	monosaccharide binding
F	0061615	biological_process	glycolytic process through fructose-6-phosphate
F	0061621	biological_process	canonical glycolysis
F	0070061	molecular_function	fructose binding
F	0070062	cellular_component	extracellular exosome
F	0070095	molecular_function	fructose-6-phosphate binding
F	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue YG1 A 801

Chain	Residue
A	MET174
A	TYR578
A	PHE670
A	TRP740
A	LEU744
A	ASP179
A	PHE308
A	ILE311
A	LYS315
A	ASN341
A	PHE537
A	ASP542
A	VAL545

site_id	AC2
Number of Residues	11
Details	binding site for residue FBP A 802

Chain	Residue
A	ALA409
A	ARG470
A	THR527
A	SER529
A	MET572
A	GLU628
A	HIS660
A	GLN663
A	ARG734
D	ARG565
D	ARG654

site_id	AC3
Number of Residues	8
Details	binding site for residue F6P A 803

Chain	Residue
A	ILE165
A	ASP166
A	MET208
A	GLU264
A	HIS298
A	ARG301
D	ARG201
D	ARG292

site_id	AC4
Number of Residues	10
Details	binding site for residue ADP A 804

Chain	Residue
A	GLY24
A	ARG88
A	CYS89
A	PHE92
A	THR93
A	GLY118
A	GLY120
A	SER121
A	GLY124
A	ILE127

site_id	AC5
Number of Residues	13
Details	binding site for residue YG1 D 801

Chain	Residue
D	MET174
D	ASP179
D	PHE308
D	ILE311
D	LYS315
D	ASN341
D	PHE537
D	ASP542
D	VAL545
D	TYR578
D	PHE670
D	TRP740
D	LEU744

site_id	AC6
Number of Residues	11
Details	binding site for residue FBP D 802

Chain	Residue
A	ARG565
A	ARG654
D	ALA409
D	ARG470
D	THR527
D	SER529
D	MET572
D	GLU628
D	HIS660
D	GLN663
D	ARG734

site_id	AC7
Number of Residues	8
Details	binding site for residue F6P D 803

Chain	Residue
A	ARG201
A	ARG292
D	ILE165
D	ASP166
D	MET208
D	GLU264
D	HIS298
D	ARG301

site_id	AC8
Number of Residues	10
Details	binding site for residue ADP D 804

Chain	Residue
D	GLY24
D	ARG88
D	CYS89
D	PHE92
D	THR93
D	GLY118
D	GLY120
D	SER121
D	GLY124
D	ILE127

site_id	AC9
Number of Residues	13
Details	binding site for residue YG1 E 801

Chain	Residue
E	MET174
E	ASP179
E	PHE308
E	ILE311
E	LYS315
E	ASN341
E	PHE537
E	ASP542
E	VAL545
E	TYR578
E	PHE670
E	TRP740
E	LEU744

site_id	AD1
Number of Residues	11
Details	binding site for residue FBP E 802

Chain	Residue
E	THR527
E	SER529
E	MET572
E	GLU628
E	HIS660
E	GLN663
E	ARG734
F	ARG565
F	ARG654
E	ALA409
E	ARG470

site_id	AD2
Number of Residues	8
Details	binding site for residue F6P E 803

Chain	Residue
E	ILE165
E	ASP166
E	MET208
E	GLU264
E	HIS298
E	ARG301
F	ARG201
F	ARG292

site_id	AD3
Number of Residues	10
Details	binding site for residue ADP E 804

Chain	Residue
E	GLY24
E	ARG88
E	CYS89
E	PHE92
E	THR93
E	GLY118
E	GLY120
E	SER121
E	GLY124
E	ILE127

site_id	AD4
Number of Residues	13
Details	binding site for residue YG1 F 801

Chain	Residue
F	MET174
F	ASP179
F	PHE308
F	ILE311
F	LYS315
F	ASN341
F	PHE537
F	ASP542
F	VAL545
F	TYR578
F	PHE670
F	TRP740
F	LEU744

site_id	AD5
Number of Residues	11
Details	binding site for residue FBP F 802

Chain	Residue
E	ARG565
E	ARG654
F	ALA409
F	ARG470
F	THR527
F	SER529
F	MET572
F	GLU628
F	HIS660
F	GLN663
F	ARG734

site_id	AD6
Number of Residues	8
Details	binding site for residue F6P F 803

Chain	Residue
E	ARG201
E	ARG292
F	ILE165
F	ASP166
F	MET208
F	GLU264
F	HIS298
F	ARG301

site_id	AD7
Number of Residues	10
Details	binding site for residue ADP F 804

Chain	Residue
F	GLY24
F	ARG88
F	CYS89
F	PHE92
F	THR93
F	GLY118
F	GLY120
F	SER121
F	GLY124
F	ILE127

Functional Information from PROSITE/UniProt

site_id	PS00433
Number of Residues	19
Details	PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGtpsafDR

Chain	Residue	Details
A	ARG292-ARG310
A	ARG654-ARG672

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_03184

Chain	Residue	Details
A	ASP166
D	ASP166
E	ASP166
F	ASP166

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_03184

Chain	Residue	Details
A	GLY25
D	ARG88
D	GLY118
D	ASP119
D	ARG201
D	ARG292
D	ARG565
D	ARG654
E	GLY25
E	ARG88
E	GLY118
A	ARG88
E	ASP119
E	ARG201
E	ARG292
E	ARG565
E	ARG654
F	GLY25
F	ARG88
F	GLY118
F	ASP119
F	ARG201
A	GLY118
F	ARG292
F	ARG565
F	ARG654
A	ASP119
A	ARG201
A	ARG292
A	ARG565
A	ARG654
D	GLY25

site_id	SWS_FT_FI3
Number of Residues	40
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_03184

Chain	Residue	Details
A	SER164
A	ARG734
D	SER164
D	MET208
D	GLU264
D	HIS298
D	ARG470
D	THR527
D	MET572
D	GLU628
D	HIS660
A	MET208
D	ARG734
E	SER164
E	MET208
E	GLU264
E	HIS298
E	ARG470
E	THR527
E	MET572
E	GLU628
E	HIS660
A	GLU264
E	ARG734
F	SER164
F	MET208
F	GLU264
F	HIS298
F	ARG470
F	THR527
F	MET572
F	GLU628
F	HIS660
A	HIS298
F	ARG734
A	ARG470
A	THR527
A	MET572
A	GLU628
A	HIS660

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0000269\|Ref.6, ECO:0007744\|PubMed:22223895, ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	ALA2
D	ALA2
E	ALA2
F	ALA2

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P47857

Chain	Residue	Details
A	SER377
D	SER377
E	SER377
F	SER377

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P12382

Chain	Residue	Details
A	TYR640
D	TYR640
E	TYR640
F	TYR640

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER775
D	SER775
E	SER775
F	SER775

site_id	SWS_FT_FI8
Number of Residues	4
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000269\|PubMed:22923583

Chain	Residue	Details
A	SER529
D	SER529
E	SER529
F	SER529

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)