1RDX
R-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI
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
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 |
Chain | Residue | Details |
A | GLU213 | |
B | GLU213 |
Chain | Residue | Details |
A | TYR244 | |
B | TYR244 |
Chain | Residue | Details |
A | PRO265 | |
B | PRO265 |
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 | 3 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
A | GLU98 | |
A | ASP68 | |
A | ASP74 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
B | GLU98 | |
B | ASP68 | |
B | 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 |