Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
| A | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006000 | biological_process | fructose metabolic process |
| A | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PDB Data
| site_id | S1 |
| Number of Residues | 8 |
| Details | WALKER-A MOTIF (GXXGXGKT), PART OF THE CLASSICAL MONONUCLEOTIDE BINDING MOTIF. |
| Chain | Residue |
| A | GLY45 |
| A | LEU46 |
| A | PRO47 |
| A | ALA48 |
| A | ARG49 |
| A | GLY50 |
| A | LYS51 |
| A | THR52 |
| site_id | S2 |
| Number of Residues | 5 |
| Details | WALKER-B MOTIF (ZZZZD, Z=HYDROPHOBIC), PART OF THE CLASSICAL MONONUCLEOTIDE BINDING MOTIF. ASP 128 SERVES AS A LIGAND TO THE MG OF MG-ATP. |
| Chain | Residue |
| A | ALA125 |
| A | VAL126 |
| A | PHE127 |
| A | ASP128 |
| A | VAL124 |
| site_id | S3 |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD FOR THE FRUCTOSE-2,6-BISPHOSPHATASE REACTION. |
| Chain | Residue |
| A | HIS256 |
| A | GLU325 |
| A | HIS390 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN |
| Chain | Residue | Details |
| A | LEU253-ASN262 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| A | ALA129 | |
| A | VAL159 | |
| Chain | Residue | Details |
| A | GLY257 | |
| Chain | Residue | Details |
| A | ILE326 | |
| Chain | Residue | Details |
| A | LEU46 | |
| A | ILE168 | |
| A | GLY428 | |
| Chain | Residue | Details |
| A | ARG79 | |
| A | ALA392 | |
| A | CYS396 | |
| A | ASN131 | |
| A | ARG137 | |
| A | GLU198 | |
| A | GLY269 | |
| A | GLU337 | |
| A | ASP351 | |
| A | TYR355 | |
| A | GLU366 | |
| Chain | Residue | Details |
| A | LYS103 | |
| A | LEU173 | |
| A | ILE194 | |
| A | HIS256 | |
| A | LEU263 | |
| A | THR306 | |
| Chain | Residue | Details |
| A | ALA348 | |
| Chain | Residue | Details |
| A | GLN391 | |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKC => ECO:0000255 |
| Chain | Residue | Details |
| A | GLN29 | |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000255 |
| Chain | Residue | Details |
| A | HIS444 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | GLU325 | |
| A | HIS390 | |
| A | ARG305 | |
| A | HIS256 | |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | GLU325 | |
| A | ASN262 | |
| A | HIS390 | |
| A | ARG255 | |
| A | ARG305 | |
| A | HIS256 | |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 810 |
| Chain | Residue | Details |
| A | HIS256 | electrostatic stabiliser |
| A | GLY257 | covalently attached, nucleofuge, nucleophile |
| A | LEU263 | electrostatic stabiliser |
| A | THR306 | electrostatic stabiliser |
| A | ILE326 | activator, proton acceptor, proton donor |
| A | GLN391 | electrostatic stabiliser |
