Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0043540 | cellular_component | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | LYS51 |
| A | THR52 |
| A | ASP128 |
| A | AGS500 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 510 |
| Chain | Residue |
| A | HIS390 |
| A | GLN391 |
| A | HOH731 |
| A | HOH918 |
| A | ARG255 |
| A | HIS256 |
| A | ASN262 |
| A | ARG305 |
| A | GLU325 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 520 |
| Chain | Residue |
| A | TYR336 |
| A | ARG350 |
| A | LYS354 |
| A | TYR365 |
| A | GLN391 |
| A | ARG395 |
| A | HOH728 |
| A | HOH730 |
| A | HOH737 |
| A | HOH915 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AGS A 500 |
| Chain | Residue |
| A | PRO47 |
| A | ALA48 |
| A | ARG49 |
| A | GLY50 |
| A | LYS51 |
| A | THR52 |
| A | TYR53 |
| A | ASN167 |
| A | GLN170 |
| A | LYS172 |
| A | VAL220 |
| A | VAL246 |
| A | TYR427 |
| A | MG501 |
| A | HOH660 |
| A | HOH688 |
| A | HOH908 |
| A | HOH909 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 530 |
| Chain | Residue |
| A | PHE299 |
| A | LEU323 |
| A | VAL375 |
| A | GLU378 |
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 | 219 |
| Details | Region: {"description":"Fructose-2,6-bisphosphatase","evidences":[{"source":"PubMed","id":"1651918","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"9890980","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9890980","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8805587","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9890980","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q16875","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07953","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00950","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]} |
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 | ARG255 | electrostatic stabiliser |
| A | HIS256 | covalently attached, nucleofuge, nucleophile |
| A | ASN262 | electrostatic stabiliser |
| A | ARG305 | electrostatic stabiliser |
| A | GLU325 | activator, proton acceptor, proton donor |
| A | HIS390 | electrostatic stabiliser |
