4FBP
CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)
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 |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0005986 | biological_process | sucrose biosynthetic process |
C | 0006000 | biological_process | fructose metabolic process |
C | 0006002 | biological_process | fructose 6-phosphate metabolic process |
C | 0006094 | biological_process | gluconeogenesis |
C | 0006111 | biological_process | regulation of gluconeogenesis |
C | 0016208 | molecular_function | AMP binding |
C | 0016311 | biological_process | dephosphorylation |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016791 | molecular_function | phosphatase activity |
C | 0030308 | biological_process | negative regulation of cell growth |
C | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
C | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
C | 0042578 | molecular_function | phosphoric ester hydrolase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0045820 | biological_process | negative regulation of glycolytic process |
C | 0046580 | biological_process | negative regulation of Ras protein signal transduction |
C | 0046872 | molecular_function | metal ion binding |
C | 0048029 | molecular_function | monosaccharide binding |
C | 0071286 | biological_process | cellular response to magnesium ion |
C | 0071466 | biological_process | cellular response to xenobiotic stimulus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0005986 | biological_process | sucrose biosynthetic process |
D | 0006000 | biological_process | fructose metabolic process |
D | 0006002 | biological_process | fructose 6-phosphate metabolic process |
D | 0006094 | biological_process | gluconeogenesis |
D | 0006111 | biological_process | regulation of gluconeogenesis |
D | 0016208 | molecular_function | AMP binding |
D | 0016311 | biological_process | dephosphorylation |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016791 | molecular_function | phosphatase activity |
D | 0030308 | biological_process | negative regulation of cell growth |
D | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
D | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
D | 0042578 | molecular_function | phosphoric ester hydrolase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0045820 | biological_process | negative regulation of glycolytic process |
D | 0046580 | biological_process | negative regulation of Ras protein signal transduction |
D | 0046872 | molecular_function | metal ion binding |
D | 0048029 | molecular_function | monosaccharide binding |
D | 0071286 | biological_process | cellular response to magnesium ion |
D | 0071466 | biological_process | cellular response to xenobiotic stimulus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AMP A 338 |
Chain | Residue |
A | VAL17 |
A | LYS112 |
A | TYR113 |
A | ARG140 |
A | VAL160 |
A | MET177 |
A | HOH628 |
A | GLN20 |
A | GLY21 |
A | ALA24 |
A | GLY26 |
A | THR27 |
A | GLU29 |
A | MET30 |
A | THR31 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AMP B 338 |
Chain | Residue |
B | VAL17 |
B | GLN20 |
B | GLY21 |
B | ALA24 |
B | GLY26 |
B | THR27 |
B | GLY28 |
B | GLU29 |
B | MET30 |
B | THR31 |
B | LYS112 |
B | TYR113 |
B | ARG140 |
B | MET177 |
B | HOH465 |
C | HOH409 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AMP C 338 |
Chain | Residue |
D | VAL17 |
D | GLN20 |
D | GLY21 |
D | THR27 |
D | GLY28 |
D | GLU29 |
D | MET30 |
D | THR31 |
D | LYS112 |
D | TYR113 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AMP D 338 |
Chain | Residue |
C | VAL17 |
C | GLN20 |
C | GLY21 |
C | GLY26 |
C | THR27 |
C | GLY28 |
C | GLU29 |
C | MET30 |
C | THR31 |
C | LYS112 |
C | TYR113 |
C | ARG140 |
C | VAL160 |
C | MET177 |
D | HOH543 |
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
Chain | Residue | Details |
A | MET18 | |
D | MET18 | |
D | GLY28 | |
D | TYR113 | |
A | GLY28 | |
A | TYR113 | |
B | MET18 | |
B | GLY28 | |
B | TYR113 | |
C | MET18 | |
C | GLY28 | |
C | TYR113 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:2164670 |
Chain | Residue | Details |
A | GLN69 | |
B | PRO119 | |
B | ASP121 | |
B | GLY122 | |
B | LYS141 | |
B | CYS281 | |
C | GLN69 | |
C | GLU98 | |
C | PRO119 | |
C | ASP121 | |
C | GLY122 | |
A | GLU98 | |
C | LYS141 | |
C | CYS281 | |
D | GLN69 | |
D | GLU98 | |
D | PRO119 | |
D | ASP121 | |
D | GLY122 | |
D | LYS141 | |
D | CYS281 | |
A | PRO119 | |
A | ASP121 | |
A | GLY122 | |
A | LYS141 | |
A | CYS281 | |
B | GLN69 | |
B | GLU98 |
Chain | Residue | Details |
A | GLU213 | |
B | GLU213 | |
C | GLU213 | |
D | GLU213 |
Chain | Residue | Details |
A | TYR244 | |
B | TYR244 | |
C | TYR244 | |
D | TYR244 |
Chain | Residue | Details |
A | PRO265 | |
B | PRO265 | |
C | PRO265 | |
D | PRO265 |
Chain | Residue | Details |
A | LEU275 | |
B | LEU275 | |
C | LEU275 | |
D | LEU275 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylthreonine => ECO:0000269|PubMed:6291465, ECO:0000269|PubMed:6296821 |
Chain | Residue | Details |
A | ASP2 | |
B | ASP2 | |
C | ASP2 | |
D | ASP2 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 |
Chain | Residue | Details |
A | ASP151 | |
B | ASP151 | |
C | ASP151 | |
D | ASP151 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:6296821 |
Chain | Residue | Details |
A | ILE208 | |
B | ILE208 | |
C | ILE208 | |
D | ILE208 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 |
Chain | Residue | Details |
A | ALA216 | |
A | VAL245 | |
B | ALA216 | |
B | VAL245 | |
C | ALA216 | |
C | VAL245 | |
D | ALA216 | |
D | VAL245 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09467 |
Chain | Residue | Details |
A | PRO265 | |
B | PRO265 | |
C | PRO265 | |
D | 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 | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
C | GLU98 | |
C | ASP74 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
D | GLU98 | |
D | ASP74 |
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 |
B | GLN69 | metal ligand, proton acceptor, proton donor |
B | VAL75 | electrostatic stabiliser, proton acceptor, proton donor |
B | GLU98 | metal ligand |
B | ASP99 | electrostatic stabiliser |
B | PRO119 | metal ligand |
B | ASP121 | metal ligand |
B | GLY122 | metal ligand |
B | CYS281 | metal ligand |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 546 |
Chain | Residue | Details |
C | GLN69 | metal ligand, proton acceptor, proton donor |
C | VAL75 | electrostatic stabiliser, proton acceptor, proton donor |
C | GLU98 | metal ligand |
C | ASP99 | electrostatic stabiliser |
C | PRO119 | metal ligand |
C | ASP121 | metal ligand |
C | GLY122 | metal ligand |
C | CYS281 | metal ligand |
site_id | MCSA4 |
Number of Residues | 8 |
Details | M-CSA 546 |
Chain | Residue | Details |
D | GLN69 | metal ligand, proton acceptor, proton donor |
D | VAL75 | electrostatic stabiliser, proton acceptor, proton donor |
D | GLU98 | metal ligand |
D | ASP99 | electrostatic stabiliser |
D | PRO119 | metal ligand |
D | ASP121 | metal ligand |
D | GLY122 | metal ligand |
D | CYS281 | metal ligand |