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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 250 |
| Chain | Residue |
| A | TRP23 |
| A | HOH252 |
| A | HOH259 |
| A | HOH284 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MLI A 990 |
| Chain | Residue |
| A | GLY22 |
| A | GLU87 |
| A | TYR90 |
| A | HOH255 |
| A | HOH268 |
| A | HOH300 |
| A | HOH304 |
| A | HOH360 |
| A | ARG8 |
| A | HIS9 |
| A | ASN15 |
| A | ARG19 |
| A | THR21 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MLI B 990 |
| Chain | Residue |
| B | ARG8 |
| B | HIS9 |
| B | ASN15 |
| B | ARG19 |
| B | THR21 |
| B | GLY22 |
| B | GLU87 |
| B | TYR90 |
| B | HOH273 |
| B | HOH322 |
| B | HOH327 |
| B | HOH359 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 250 |
| Chain | Residue |
| A | EDO251 |
| B | ARG63 |
| B | TRP66 |
| B | HIS67 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 251 |
| Chain | Residue |
| A | ARG63 |
| A | HIS67 |
| B | EDO250 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 251 |
| Chain | Residue |
| A | VAL79 |
| A | HOH260 |
| B | PRO78 |
| B | VAL79 |
| B | ARG115 |
| B | HOH289 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21904048","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21904048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FDZ","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]} |
