1X9I
Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| A | 0004476 | molecular_function | mannose-6-phosphate isomerase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0097367 | molecular_function | carbohydrate derivative binding |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| B | 0004476 | molecular_function | mannose-6-phosphate isomerase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008152 | biological_process | metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0097367 | molecular_function | carbohydrate derivative binding |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE G6Q A 600 |
| Chain | Residue |
| A | MET45 |
| A | ARG135 |
| A | GLU203 |
| A | LYS298 |
| A | HOH721 |
| A | HOH763 |
| A | HOH931 |
| A | HOH938 |
| B | HIS219 |
| A | GLY46 |
| A | GLY47 |
| A | SER48 |
| A | SER87 |
| A | TYR88 |
| A | SER89 |
| A | THR92 |
| A | PRO134 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE G6Q B 601 |
| Chain | Residue |
| A | HIS219 |
| B | MET45 |
| B | GLY46 |
| B | GLY47 |
| B | SER48 |
| B | SER87 |
| B | TYR88 |
| B | SER89 |
| B | THR92 |
| B | PRO134 |
| B | ARG135 |
| B | GLU203 |
| B | LYS298 |
| B | HOH626 |
| B | HOH796 |
| B | HOH797 |
| B | HOH803 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 701 |
| Chain | Residue |
| A | ASP53 |
| A | LYS72 |
| A | ARG191 |
| A | TYR195 |
| A | HOH737 |
| A | HOH749 |
| A | HOH784 |
| A | HOH859 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 702 |
| Chain | Residue |
| A | ALA70 |
| A | VAL71 |
| A | LYS72 |
| A | ASP73 |
| A | HOH851 |
| A | HOH859 |
| B | ARG56 |
| B | GLU188 |
| B | HOH776 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU203 | |
| A | LYS298 | |
| B | GLU203 | |
| B | LYS298 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305 |
| Chain | Residue | Details |
| A | HIS219 | |
| B | HIS219 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER48 | |
| A | SER87 | |
| A | THR92 | |
| B | SER48 | |
| B | SER87 | |
| B | THR92 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 736 |
| Chain | Residue | Details |
| A | ARG135 | electrostatic stabiliser |
| A | GLU203 | proton acceptor, proton donor |
| A | HIS219 | proton acceptor, proton donor |
| A | LYS298 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 736 |
| Chain | Residue | Details |
| B | ARG135 | electrostatic stabiliser |
| B | GLU203 | proton acceptor, proton donor |
| B | HIS219 | proton acceptor, proton donor |
| B | LYS298 | proton acceptor, proton donor |
