Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016829 | molecular_function | lyase activity |
| C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016829 | molecular_function | lyase activity |
| D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT A 400 |
| Chain | Residue |
| A | LYS143 |
| A | HOH458 |
| A | HOH750 |
| A | HOH866 |
| A | GLU186 |
| A | LYS228 |
| A | LEU269 |
| A | SER270 |
| A | GLY271 |
| A | SER298 |
| A | GLY300 |
| A | ARG301 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CIT B 400 |
| Chain | Residue |
| B | LYS143 |
| B | ARG145 |
| B | GLU186 |
| B | LYS228 |
| B | LEU269 |
| B | SER270 |
| B | GLY271 |
| B | SER298 |
| B | GLY300 |
| B | ARG301 |
| B | HOH399 |
| B | HOH453 |
| B | HOH464 |
| B | HOH644 |
| B | HOH760 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT C 400 |
| Chain | Residue |
| C | ARG40 |
| C | LYS143 |
| C | GLU186 |
| C | LYS228 |
| C | LEU269 |
| C | SER270 |
| C | GLY271 |
| C | SER298 |
| C | GLY300 |
| C | ARG301 |
| C | HOH836 |
| C | HOH837 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 400 |
| Chain | Residue |
| D | LYS228 |
| D | GLY300 |
| D | ARG301 |
| D | HOH882 |
| D | HOH885 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 401 |
| Chain | Residue |
| A | LYS219 |
| A | VAL220 |
| A | HOH445 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 401 |
| Chain | Residue |
| B | ASN216 |
| B | LYS219 |
| B | VAL220 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 402 |
| Chain | Residue |
| B | LYS68 |
| B | TYR69 |
| B | MET326 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 401 |
| Chain | Residue |
| C | ASN216 |
| C | LYS219 |
| C | VAL220 |
| D | ARG257 |
| D | HOH409 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG C 402 |
| Chain | Residue |
| C | LYS64 |
| C | LYS68 |
| C | TYR69 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG D 401 |
| Chain | Residue |
| D | ASN216 |
| D | LYS219 |
| D | VAL220 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG D 402 |
| Chain | Residue |
| D | LYS64 |
| D | LYS68 |
| D | TYR69 |
| D | HOH619 |
Functional Information from PROSITE/UniProt
| site_id | PS00158 |
| Number of Residues | 11 |
| Details | ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. VlLEGaLLKPN |
| Chain | Residue | Details |
| A | VAL220-ASN230 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| A | ASP31 | |
| A | LYS228 | |
| A | GLU186 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| B | ASP31 | |
| B | LYS228 | |
| B | GLU186 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| C | ASP31 | |
| C | LYS228 | |
| C | GLU186 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| D | ASP31 | |
| D | LYS228 | |
| D | GLU186 | |
