1DCU
REDOX SIGNALING IN THE CHLOROPLAST: STRUCTURE OF OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATE PHOSPHATASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
| A | 0042578 | molecular_function | phosphoric ester hydrolase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
| B | 0042578 | molecular_function | phosphoric ester hydrolase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016791 | molecular_function | phosphatase activity |
| C | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
| C | 0042578 | molecular_function | phosphoric ester hydrolase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016791 | molecular_function | phosphatase activity |
| D | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
| D | 0042578 | molecular_function | phosphoric ester hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00124 |
| Number of Residues | 13 |
| Details | FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcaPMS |
| Chain | Residue | Details |
| A | GLY298-SER310 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU76 | |
| A | LYS299 | |
| A | GLU305 | |
| B | GLU76 | |
| B | GLU105 | |
| B | ASP126 | |
| B | LEU128 | |
| B | ASP129 | |
| B | ASN237 | |
| B | TYR269 | |
| B | TYR287 | |
| A | GLU105 | |
| B | TYR289 | |
| B | LYS299 | |
| B | GLU305 | |
| C | GLU76 | |
| C | GLU105 | |
| C | ASP126 | |
| C | LEU128 | |
| C | ASP129 | |
| C | ASN237 | |
| C | TYR269 | |
| A | ASP126 | |
| C | TYR287 | |
| C | TYR289 | |
| C | LYS299 | |
| C | GLU305 | |
| D | GLU76 | |
| D | GLU105 | |
| D | ASP126 | |
| D | LEU128 | |
| D | ASP129 | |
| D | ASN237 | |
| A | LEU128 | |
| D | TYR269 | |
| D | TYR287 | |
| D | TYR289 | |
| D | LYS299 | |
| D | GLU305 | |
| A | ASP129 | |
| A | ASN237 | |
| A | TYR269 | |
| A | TYR287 | |
| A | TYR289 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eyi |
| Chain | Residue | Details |
| A | GLU106 | |
| A | GLU76 | |
| A | ASP82 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eyi |
| Chain | Residue | Details |
| B | GLU106 | |
| B | GLU76 | |
| B | ASP82 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eyi |
| Chain | Residue | Details |
| C | GLU106 | |
| C | GLU76 | |
| C | ASP82 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eyi |
| Chain | Residue | Details |
| D | GLU106 | |
| D | GLU76 | |
| D | ASP82 |
