4GWY
Crystal Structure of AMP Complexes of Porcine Liver Fructose-1,6-bisphosphatase with Blocked Subunit Pair Rotation
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 |
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 | VAL17 | |
A | THR27 | |
A | LYS112 |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:2164670 |
Chain | Residue | Details |
A | ASP68 | |
A | GLU97 | |
A | ASP118 | |
A | LEU120 | |
A | ASP121 | |
A | ARG140 | |
A | GLU280 |
Chain | Residue | Details |
A | ASN212 |
Chain | Residue | Details |
A | ARG243 |
Chain | Residue | Details |
A | TYR264 |
Chain | Residue | Details |
A | LYS274 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylthreonine => ECO:0000269|PubMed:6291465, ECO:0000269|PubMed:6296821 |
Chain | Residue | Details |
A | THR1 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 |
Chain | Residue | Details |
A | LYS150 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:6296821 |
Chain | Residue | Details |
A | SER207 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 |
Chain | Residue | Details |
A | TYR215 | |
A | TYR244 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09467 |
Chain | Residue | Details |
A | 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 |