Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1FPL

FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND THALLIUM IONS (10 MM)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0003824	molecular_function	catalytic activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006000	biological_process	fructose metabolic process
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006111	biological_process	regulation of gluconeogenesis
A	0016208	molecular_function	AMP binding
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0030308	biological_process	negative regulation of cell growth
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0042132	molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity
A	0042578	molecular_function	phosphoric ester hydrolase activity
A	0042802	molecular_function	identical protein binding
A	0045820	biological_process	negative regulation of glycolytic process
A	0046580	biological_process	negative regulation of Ras protein signal transduction
A	0046872	molecular_function	metal ion binding
A	0048029	molecular_function	monosaccharide binding
A	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
A	0071286	biological_process	cellular response to magnesium ion
A	0071466	biological_process	cellular response to xenobiotic stimulus
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0003824	molecular_function	catalytic activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006000	biological_process	fructose metabolic process
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006111	biological_process	regulation of gluconeogenesis
B	0016208	molecular_function	AMP binding
B	0016787	molecular_function	hydrolase activity
B	0016791	molecular_function	phosphatase activity
B	0030308	biological_process	negative regulation of cell growth
B	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
B	0042132	molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity
B	0042578	molecular_function	phosphoric ester hydrolase activity
B	0042802	molecular_function	identical protein binding
B	0045820	biological_process	negative regulation of glycolytic process
B	0046580	biological_process	negative regulation of Ras protein signal transduction
B	0046872	molecular_function	metal ion binding
B	0048029	molecular_function	monosaccharide binding
B	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
B	0071286	biological_process	cellular response to magnesium ion
B	0071466	biological_process	cellular response to xenobiotic stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	ACTIVE SITE IN THE MONOMER COMPOSED OF CHAINS A.

Chain	Residue
B	ARG243
A	TYR244
A	ASN212
A	TYR215
A	TYR264
A	LYS274
A	MET248
A	ARG276
A	GLU280
A	GLY122
A	ASP121

site_id	AC2
Number of Residues	11
Details	ACTIVE SITE IN THE MONOMER COMPOSED OF CHAINS B.

Chain	Residue
A	ARG243
B	TYR244
B	ASN212
B	TYR215
B	TYR264
B	LYS274
B	MET248
B	ARG276
B	GLU280
B	GLY122
B	ASP121

site_id	AM1
Number of Residues	13
Details	AMP BINDING SITE IN THE MONOMER COMPOSED OF CHAINS A.

Chain	Residue
A	GLN20
A	MET177
A	ALA24
A	GLY21
A	GLY26
A	VAL17
A	THR31
A	ARG140
A	TYR113
A	GLU29
A	MET30
A	THR27
A	LYS112

site_id	AM2
Number of Residues	13
Details	AMP BINDING SITE IN THE MONOMER COMPOSED OF CHAINS B.

Chain	Residue
B	GLN20
B	VAL17
B	THR31
B	ARG140
B	TYR113
B	GLU29
B	MET30
B	THR27
B	LYS112
B	MET177
B	ALA24
B	GLY21
B	GLY26

site_id	TH1
Number of Residues	4
Details	FIRST METAL SITE IN THE MONOMER COMPOSED OF CHAINS A.

Chain	Residue
A	GLU97
A	ASP118
A	GLU280
A	ASP121

site_id	TH2
Number of Residues	4
Details	FIRST METAL SITE IN THE MONOMER COMPOSED OF CHAINS B.

Chain	Residue
B	GLU97
B	ASP118
B	GLU280
B	ASP121

site_id	TH3
Number of Residues	4
Details	SECOND METAL SITE IN THE MONOMER COMPOSED OF CHAINS A.

Chain	Residue
A	GLU97
A	ASP118
A	LEU120
A	GLU98

site_id	TH4
Number of Residues	4
Details	SECOND METAL SITE IN THE MONOMER COMPOSED OF CHAINS B.

Chain	Residue
B	GLU97
B	ASP118
B	LEU120
B	GLU98

site_id	TH5
Number of Residues	2
Details	THIRD METAL SITE IN THE MONOMER COMPOSED OF CHAINS A.

Chain	Residue
A	GLU280
A	ARG276

site_id	TH6
Number of Residues	2
Details	THIRD METAL SITE IN THE MONOMER COMPOSED OF CHAINS B.

Chain	Residue
B	GLU280
B	ARG276

Functional Information from PROSITE/UniProt

site_id	PS00124
Number of Residues	13
Details	FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA

Chain	Residue	Details
A	GLY273-ALA285

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FPD, ECO:0007744\|PDB:1FPE, ECO:0007744\|PDB:1FPF, ECO:0007744\|PDB:1FPG, ECO:0007744\|PDB:1FPI, ECO:0007744\|PDB:1FPJ, ECO:0007744\|PDB:1FPL, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4FBP, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP

Chain	Residue	Details
A	MET18
A	GLY28
A	TYR113
B	MET18
B	GLY28
B	TYR113

site_id	SWS_FT_FI2
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269\|PubMed:2164670

Chain	Residue	Details
A	GLN69
B	PRO119
B	ASP121
B	GLY122
B	LYS141
B	CYS281
A	GLU98
A	PRO119
A	ASP121
A	GLY122
A	LYS141
A	CYS281
B	GLN69
B	GLU98

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV6, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:2QVU, ECO:0007744\|PDB:2QVV, ECO:0007744\|PDB:3FBP, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWU, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP

Chain	Residue	Details
A	GLU213
B	GLU213

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV6, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP

Chain	Residue	Details
A	TYR244
B	TYR244

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FPB, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV6, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:2QVU, ECO:0007744\|PDB:2QVV, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWU, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP

Chain	Residue	Details
A	PRO265
B	PRO265

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP

Chain	Residue	Details
A	LEU275
B	LEU275

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N-acetylthreonine => ECO:0000269\|PubMed:6291465, ECO:0000269\|PubMed:6296821

Chain	Residue	Details
A	ASP2
B	ASP2

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q9QXD6

Chain	Residue	Details
A	ASP151
B	ASP151

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269\|PubMed:6296821

Chain	Residue	Details
A	ILE208
B	ILE208

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:Q9QXD6

Chain	Residue	Details
A	ALA216
A	VAL245
B	ALA216
B	VAL245

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P09467

Chain	Residue	Details
A	PRO265
B	PRO265

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1eyi

Chain	Residue	Details
A	GLU98
A	ASP74

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1eyi

Chain	Residue	Details
B	GLU98
B	ASP74

site_id	MCSA1
Number of Residues	7
Details	M-CSA 546

Chain	Residue	Details
A	ASP74	electrostatic stabiliser, proton acceptor, proton donor
A	GLU97	metal ligand
A	GLU98	electrostatic stabiliser
A	ASP118	metal ligand
A	LEU120	metal ligand
A	ASP121	metal ligand
A	GLU280	metal ligand

site_id	MCSA2
Number of Residues	7
Details	M-CSA 546

Chain	Residue	Details
B	ASP74	electrostatic stabiliser, proton acceptor, proton donor
B	GLU97	metal ligand
B	GLU98	electrostatic stabiliser
B	ASP118	metal ligand
B	LEU120	metal ligand
B	ASP121	metal ligand
B	GLU280	metal ligand

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