Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004619 | molecular_function | phosphoglycerate mutase activity |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| B | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 A 250 |
| Chain | Residue |
| A | ASP51 |
| A | PRO78 |
| A | LYS175 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 251 |
| Chain | Residue |
| A | TYR227 |
| A | ILE190 |
| A | ASP194 |
| A | ILE196 |
| A | LEU204 |
| A | TYR214 |
| A | HIS225 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 250 |
| Chain | Residue |
| B | ASP51 |
| B | GLY174 |
| B | LYS175 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 B 251 |
| Chain | Residue |
| B | ILE190 |
| B | ASP194 |
| B | TYR214 |
| B | HIS225 |
| B | TYR227 |
| B | HOH357 |
| B | HOH426 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsTwN |
| Chain | Residue | Details |
| A | LEU6-ASN15 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS9 | |
| B | HIS9 | |
| Chain | Residue | Details |
| A | GLU87 | |
| B | GLU87 | |
| Chain | Residue | Details |
| A | ARG8 | |
| A | ARG114 | |
| A | ARG115 | |
| A | HIS182 | |
| A | GLY183 | |
| A | ASN184 | |
| B | ARG8 | |
| B | HIS9 | |
| B | ASN15 | |
| B | THR21 | |
| B | GLY22 | |
| A | HIS9 | |
| B | ARG60 | |
| B | GLU87 | |
| B | TYR90 | |
| B | LYS98 | |
| B | ARG114 | |
| B | ARG115 | |
| B | HIS182 | |
| B | GLY183 | |
| B | ASN184 | |
| A | ASN15 | |
| A | THR21 | |
| A | GLY22 | |
| A | ARG60 | |
| A | GLU87 | |
| A | TYR90 | |
| A | LYS98 | |
| Chain | Residue | Details |
| A | HIS182 | |
| B | HIS182 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | HIS182 | |
| A | ARG60 | |
| A | GLU87 | |
| A | HIS9 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| B | HIS182 | |
| B | ARG60 | |
| B | GLU87 | |
| B | HIS9 | |
