5UM0
Crystal structure of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Neisseria gonorrhoeae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 |
| C | 0004619 | molecular_function | phosphoglycerate mutase activity |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| D | 0004619 | molecular_function | phosphoglycerate mutase activity |
| D | 0006094 | biological_process | gluconeogenesis |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016868 | molecular_function | intramolecular phosphotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue TLA A 300 |
| Chain | Residue |
| A | ARG7 |
| A | HOH403 |
| A | HOH409 |
| A | HOH423 |
| A | HOH442 |
| A | HOH447 |
| A | HOH459 |
| A | HOH528 |
| A | HOH554 |
| A | ASN14 |
| A | LEU18 |
| A | PHE19 |
| A | THR20 |
| A | GLY21 |
| A | GLU86 |
| A | TYR89 |
| A | LYS97 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue TLA B 300 |
| Chain | Residue |
| B | ARG7 |
| B | PHE19 |
| B | THR20 |
| B | GLY21 |
| B | GLU86 |
| B | LYS97 |
| B | ASN183 |
| B | HOH454 |
| B | HOH457 |
| B | HOH473 |
| B | HOH529 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue TLA C 300 |
| Chain | Residue |
| C | ARG7 |
| C | ASN14 |
| C | LEU18 |
| C | PHE19 |
| C | THR20 |
| C | GLY21 |
| C | GLU86 |
| C | TYR89 |
| C | LYS97 |
| C | ASN183 |
| C | HOH403 |
| C | HOH424 |
| C | HOH447 |
| C | HOH450 |
| C | HOH504 |
| C | HOH518 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue TLA D 300 |
| Chain | Residue |
| D | ARG7 |
| D | PHE19 |
| D | THR20 |
| D | GLY21 |
| D | GLU86 |
| D | TYR89 |
| D | LYS97 |
| D | ARG113 |
| D | HOH411 |
| D | HOH416 |
| D | HOH418 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
