Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1LEV

PORCINE KIDNEY FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH AN AMP-SITE INHIBITOR

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0005986	biological_process	sucrose biosynthetic 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	0008152	biological_process	metabolic process
A	0016208	molecular_function	AMP binding
A	0016311	biological_process	dephosphorylation
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	0071286	biological_process	cellular response to magnesium ion
A	0071466	biological_process	cellular response to xenobiotic stimulus
F	0003824	molecular_function	catalytic activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005975	biological_process	carbohydrate metabolic process
F	0005986	biological_process	sucrose biosynthetic process
F	0006000	biological_process	fructose metabolic process
F	0006002	biological_process	fructose 6-phosphate metabolic process
F	0006094	biological_process	gluconeogenesis
F	0006111	biological_process	regulation of gluconeogenesis
F	0008152	biological_process	metabolic process
F	0016208	molecular_function	AMP binding
F	0016311	biological_process	dephosphorylation
F	0016787	molecular_function	hydrolase activity
F	0016791	molecular_function	phosphatase activity
F	0030308	biological_process	negative regulation of cell growth
F	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
F	0042132	molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity
F	0042578	molecular_function	phosphoric ester hydrolase activity
F	0042802	molecular_function	identical protein binding
F	0045820	biological_process	negative regulation of glycolytic process
F	0046580	biological_process	negative regulation of Ras protein signal transduction
F	0046872	molecular_function	metal ion binding
F	0048029	molecular_function	monosaccharide binding
F	0071286	biological_process	cellular response to magnesium ion
F	0071466	biological_process	cellular response to xenobiotic stimulus

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
F	MET18
F	GLY28
F	TYR113

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

Chain	Residue	Details
A	GLN69
F	PRO119
F	ASP121
F	GLY122
F	LYS141
F	CYS281
A	GLU98
A	PRO119
A	ASP121
A	GLY122
A	LYS141
A	CYS281
F	GLN69
F	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
F	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
F	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
F	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
F	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
F	ASP2

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

Chain	Residue	Details
A	ASP151
F	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
F	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
F	ALA216
F	VAL245

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

Chain	Residue	Details
A	PRO265
F	PRO265

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 546

Chain	Residue	Details
A	GLN69	metal ligand, proton acceptor, proton donor
A	VAL75	electrostatic stabiliser, proton acceptor, proton donor
A	GLU98	metal ligand
A	ASP99	electrostatic stabiliser
A	PRO119	metal ligand
A	ASP121	metal ligand
A	GLY122	metal ligand
A	CYS281	metal ligand

site_id	MCSA2
Number of Residues	8
Details	M-CSA 546

Chain	Residue	Details
F	GLN69	metal ligand, proton acceptor, proton donor
F	VAL75	electrostatic stabiliser, proton acceptor, proton donor
F	GLU98	metal ligand
F	ASP99	electrostatic stabiliser
F	PRO119	metal ligand
F	ASP121	metal ligand
F	GLY122	metal ligand
F	CYS281	metal ligand

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