2QVR
E. coli Fructose-1,6-bisphosphatase: Citrate, Fru-2,6-P2, and Mg2+ bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0008152 | biological_process | metabolic process |
| A | 0016051 | biological_process | carbohydrate biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0032991 | cellular_component | protein-containing complex |
| 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 | 0046872 | molecular_function | metal ion binding |
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 | GLY268-ALA280 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17314096, ECO:0007744|PDB:2OX3 |
| Chain | Residue | Details |
| A | THR3 | |
| A | LYS30 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17567577, ECO:0007744|PDB:2Q8M |
| Chain | Residue | Details |
| A | THR19 | |
| A | LYS104 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:17567577 |
| Chain | Residue | Details |
| A | GLU89 | |
| A | LEU112 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:17567577, ECO:0000269|PubMed:17933867 |
| Chain | Residue | Details |
| A | ASP110 | |
| A | ASP113 | |
| A | GLU275 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17933867, ECO:0007744|PDB:2OWZ, ECO:0007744|PDB:2QVR |
| Chain | Residue | Details |
| A | PHE187 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17567577 |
| Chain | Residue | Details |
| A | ASN206 | |
| A | TYR239 | |
| A | TYR257 | |
| A | LYS269 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17567577, ECO:0007744|PDB:2Q8M |
| Chain | Residue | Details |
| A | LYS222 | |
| A | GLN225 |
