Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5HTK

Human Heart 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase (PFKFB2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003873	molecular_function	6-phosphofructo-2-kinase activity
A	0004331	molecular_function	fructose-2,6-bisphosphate 2-phosphatase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0006000	biological_process	fructose metabolic process
A	0006003	biological_process	fructose 2,6-bisphosphate metabolic process
A	0006007	biological_process	glucose catabolic process
A	0006089	biological_process	lactate metabolic process
A	0006090	biological_process	pyruvate metabolic process
A	0006096	biological_process	glycolytic process
A	0009749	biological_process	response to glucose
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016787	molecular_function	hydrolase activity
A	0019900	molecular_function	kinase binding
A	0019901	molecular_function	protein kinase binding
A	0032024	biological_process	positive regulation of insulin secretion
A	0046835	biological_process	carbohydrate phosphorylation
B	0003824	molecular_function	catalytic activity
B	0003873	molecular_function	6-phosphofructo-2-kinase activity
B	0004331	molecular_function	fructose-2,6-bisphosphate 2-phosphatase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005654	cellular_component	nucleoplasm
B	0005829	cellular_component	cytosol
B	0006000	biological_process	fructose metabolic process
B	0006003	biological_process	fructose 2,6-bisphosphate metabolic process
B	0006007	biological_process	glucose catabolic process
B	0006089	biological_process	lactate metabolic process
B	0006090	biological_process	pyruvate metabolic process
B	0006096	biological_process	glycolytic process
B	0009749	biological_process	response to glucose
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
B	0016787	molecular_function	hydrolase activity
B	0019900	molecular_function	kinase binding
B	0019901	molecular_function	protein kinase binding
B	0032024	biological_process	positive regulation of insulin secretion
B	0046835	biological_process	carbohydrate phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00175
Number of Residues	10
Details	PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsEfN

Chain	Residue	Details
A	LEU254-ASN263

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255

Chain	Residue	Details
A	ASP128
A	CYS158
B	ASP128
B	CYS158

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250\|UniProtKB:Q16875

Chain	Residue	Details
A	NEP257
B	NEP257

site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250\|UniProtKB:Q16875

Chain	Residue	Details
A	GLU326
B	GLU326

site_id	SWS_FT_FI4
Number of Residues	36
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q16875

Chain	Residue	Details
A	GLY45
A	ARG256
A	ASN263
A	GLY269
A	TYR337
A	ARG351
A	LYS355
A	TYR366
A	GLN392
A	TYR428
B	GLY45
A	ARG78
B	ARG78
B	ARG102
B	THR130
B	ARG136
B	ASN167
B	LYS172
B	ARG193
B	TYR197
B	ARG256
B	ASN263
A	ARG102
B	GLY269
B	TYR337
B	ARG351
B	LYS355
B	TYR366
B	GLN392
B	TYR428
A	THR130
A	ARG136
A	ASN167
A	LYS172
A	ARG193
A	TYR197

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P07953

Chain	Residue	Details
A	PHE348
A	ARG396
B	PHE348
B	ARG396

site_id	SWS_FT_FI6
Number of Residues	6
Details	SITE: Transition state stabilizer => ECO:0000250\|UniProtKB:Q16875

Chain	Residue	Details
A	ARG256
A	ASN263
A	HIS391
B	ARG256
B	ASN263
B	HIS391

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	SER2
B	SER2

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000250

Chain	Residue	Details
A	SER29
B	SER29

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine; by AMPK => ECO:0000269\|PubMed:11069105, ECO:0000269\|PubMed:36402789, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER466
B	SER466

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:36402789, ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	THR468
B	THR468

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	THR475
B	THR475

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphoserine; by BRAF => ECO:0000269\|PubMed:36402789, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
A	SER483
B	SER483

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:36402789

Chain	Residue	Details
A	SER486
B	SER486

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:36402789, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER493
B	SER493

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