Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 400 |
| Chain | Residue |
| B | ARG8 |
| B | HIS9 |
| B | ASN15 |
| B | ARG58 |
| B | GLU78 |
| B | HIS143 |
| B | GLN144 |
| B | GTP355 |
| B | HOH402 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | ARG8 |
| A | HIS9 |
| A | ASN15 |
| A | ARG58 |
| A | GLU78 |
| A | HIS143 |
| A | GLN144 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GTP B 355 |
| Chain | Residue |
| A | GTP356 |
| A | HOH534 |
| B | ILE20 |
| B | GLU78 |
| B | ILE79 |
| B | TYR89 |
| B | PHE100 |
| B | ARG103 |
| B | LYS107 |
| B | TYR112 |
| B | TYR118 |
| B | GLN144 |
| B | ALA145 |
| B | ARG148 |
| B | PRO163 |
| B | PO4400 |
| B | HOH444 |
| B | HOH470 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GTP A 356 |
| Chain | Residue |
| A | ILE20 |
| A | GLU78 |
| A | ILE79 |
| A | TYR89 |
| A | PHE100 |
| A | ARG103 |
| A | TYR112 |
| A | TYR118 |
| A | GLN144 |
| A | ALA145 |
| A | ARG148 |
| A | PRO163 |
| A | HOH431 |
| A | HOH443 |
| A | HOH518 |
| A | HOH534 |
| B | GTP355 |
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 | LEU6-ASN15 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLY10 | |
| B | GLY10 | |
| Chain | Residue | Details |
| A | ILE79 | |
| B | ILE79 | |
| Chain | Residue | Details |
| A | HIS9 | |
| A | LEU16 | |
| A | THR59 | |
| A | GLY181 | |
| B | HIS9 | |
| B | LEU16 | |
| B | THR59 | |
| B | GLY181 | |
| Chain | Residue | Details |
| A | GLY22 | |
| B | ASP104 | |
| B | TYR108 | |
| B | GLU119 | |
| B | ALA145 | |
| B | CYS149 | |
| A | GLU90 | |
| A | ASP104 | |
| A | TYR108 | |
| A | GLU119 | |
| A | ALA145 | |
| A | CYS149 | |
| B | GLY22 | |
| B | GLU90 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|Ref.15 |
| Chain | Residue | Details |
| A | ALA101 | |
| B | ALA101 | |
| Chain | Residue | Details |
| A | GLN144 | |
| B | GLN144 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | ARG58 | |
| A | HIS143 | |
| A | GLU78 | |
| A | HIS9 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| B | ARG58 | |
| B | HIS143 | |
| B | GLU78 | |
| B | HIS9 | |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | ARG58 | |
| A | ASN15 | |
| A | ARG8 | |
| A | HIS143 | |
| A | GLU78 | |
| A | HIS9 | |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| B | ARG58 | |
| B | ASN15 | |
| B | ARG8 | |
| B | HIS143 | |
| B | GLU78 | |
| B | HIS9 | |
