Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4GX6

AMP Complexes of Porcine Liver Fructose-1,6-bisphosphatase with Mutation E192Q

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0005986	biological_process	sucrose biosynthetic 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	0016311	biological_process	dephosphorylation
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	0071286	biological_process	cellular response to magnesium ion
B	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	VAL17
A	THR27
A	LYS112
B	VAL17
B	THR27
B	LYS112

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

Chain	Residue	Details
A	ASP118
A	LEU120
A	ASP121
A	ARG140
A	GLU280
B	ASP68
B	GLU97
B	ASP118
B	LEU120
B	ASP121
B	ARG140
B	GLU280
A	ASP68
A	GLU97

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
B	ASN212
A	ASN212

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
B	ARG243
A	ARG243

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
B	TYR264
A	TYR264

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
B	LYS274
A	LYS274

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
B	THR1
A	THR1

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

Chain	Residue	Details
B	LYS150
A	LYS150

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

Chain	Residue	Details
B	SER207
A	SER207

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

Chain	Residue	Details
B	TYR215
B	TYR244
A	TYR215
A	TYR244

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

Chain	Residue	Details
A	TYR264
B	TYR264

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 546

Chain	Residue	Details
A	ASP68	metal ligand, proton acceptor, proton donor
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	8
Details	M-CSA 546

Chain	Residue	Details
B	ASP68	metal ligand, proton acceptor, proton donor
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)
		EDMap 2fo-fc (MTZ)