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 | 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 | 0016853 | molecular_function | isomerase activity |
A | 0097367 | molecular_function | carbohydrate derivative binding |
A | 1901135 | biological_process | carbohydrate derivative metabolic process |
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 | 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 | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1x9h |
Chain | Residue | Details |
A | ARG135 | |
A | LYS298 | |
A | HIS219 | |
A | GLU203 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1x9h |
Chain | Residue | Details |
B | ARG135 | |
B | LYS298 | |
B | HIS219 | |
B | GLU203 |
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 |