Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016829 | molecular_function | lyase activity |
A | 0016832 | molecular_function | aldehyde-lyase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016829 | molecular_function | lyase activity |
B | 0016832 | molecular_function | aldehyde-lyase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ZN A 1005 |
Chain | Residue |
A | HIS110 |
A | GLU174 |
A | HIS226 |
A | HIS264 |
A | HOH1116 |
A | HOH1122 |
A | HOH1291 |
A | HOH1433 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NH4 A 1006 |
Chain | Residue |
A | HIS107 |
A | ASP109 |
A | MET142 |
A | GLU172 |
A | HIS264 |
A | LYS284 |
A | ASN286 |
A | GLN59 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN B 1323 |
Chain | Residue |
B | HIS110 |
B | GLU174 |
B | HIS226 |
B | HIS264 |
B | HOH1782 |
B | HOH1783 |
B | HOH1793 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NH4 B 1324 |
Chain | Residue |
B | GLN59 |
B | HIS107 |
B | ASP109 |
B | GLU172 |
B | LYS284 |
B | ASN286 |
Functional Information from PROSITE/UniProt
site_id | PS00602 |
Number of Residues | 12 |
Details | ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC |
Chain | Residue | Details |
A | TYR100-CYS111 | |
site_id | PS00806 |
Number of Residues | 12 |
Details | ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE |
Chain | Residue | Details |
A | LEU171-GLU182 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS110 | |
B | HIS110 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ASN62 | |
B | ASN62 | |
Chain | Residue | Details |
A | CYS111 | |
B | GLY265 | |
A | LEU145 | |
A | LEU175 | |
A | GLY227 | |
A | GLY265 | |
B | CYS111 | |
B | LEU145 | |
B | LEU175 | |
B | GLY227 | |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | VAL228 | |
A | GLY266 | |
A | ILE287 | |
B | VAL228 | |
B | GLY266 | |
B | ILE287 | |
Chain | Residue | Details |
A | PRO9 | |
B | PRO9 | |
Chain | Residue | Details |
A | GLY72 | |
B | ALA231 | |
B | LYS251 | |
B | GLY319 | |
B | LYS326 | |
B | ALA348 | |
A | LEU115 | |
A | ALA231 | |
A | LYS251 | |
A | GLY319 | |
A | LYS326 | |
A | ALA348 | |
B | GLY72 | |
B | LEU115 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b57 |
Chain | Residue | Details |
A | ASP109 | |
A | ASN286 | |
A | GLU182 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b57 |
Chain | Residue | Details |
B | ASP109 | |
B | ASN286 | |
B | GLU182 | |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
A | HIS110 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | CYS111 | metal ligand |
A | ASP183 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLY227 | metal ligand |
A | GLY265 | metal ligand |
A | ILE287 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
B | HIS110 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | CYS111 | metal ligand |
B | ASP183 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLY227 | metal ligand |
B | GLY265 | metal ligand |
B | ILE287 | electrostatic stabiliser, hydrogen bond donor, steric role |