1RYE
Crystal Structure of the Shifted Form of the Glucose-Fructose Oxidoreductase from Zymomonas mobilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006061 | biological_process | sorbitol biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0047061 | molecular_function | glucose-fructose oxidoreductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006061 | biological_process | sorbitol biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0047061 | molecular_function | glucose-fructose oxidoreductase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0006061 | biological_process | sorbitol biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0047061 | molecular_function | glucose-fructose oxidoreductase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0006061 | biological_process | sorbitol biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0047061 | molecular_function | glucose-fructose oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP A 500 |
| Chain | Residue |
| A | GLY38 |
| A | ILE105 |
| A | LEU106 |
| A | PRO107 |
| A | ASN108 |
| A | HIS111 |
| A | GLU128 |
| A | LYS129 |
| A | GLY155 |
| A | ARG157 |
| A | ALA196 |
| A | LEU39 |
| A | TRP199 |
| A | ARG200 |
| A | TYR217 |
| A | TYR296 |
| A | HOH606 |
| A | HOH622 |
| A | HOH637 |
| A | HOH641 |
| A | HOH644 |
| A | HOH645 |
| A | GLY40 |
| D | PRO11 |
| D | THR13 |
| D | PRO14 |
| D | ALA15 |
| D | GLY16 |
| D | ARG17 |
| A | LYS41 |
| A | TYR42 |
| A | SER64 |
| A | GLY65 |
| A | LYS69 |
| A | TYR87 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NDP B 501 |
| Chain | Residue |
| B | LEU39 |
| B | GLY40 |
| B | LYS41 |
| B | TYR42 |
| B | SER64 |
| B | GLY65 |
| B | LYS69 |
| B | TYR87 |
| B | ILE105 |
| B | LEU106 |
| B | PRO107 |
| B | ASN108 |
| B | LEU110 |
| B | HIS111 |
| B | GLU128 |
| B | LYS129 |
| B | ARG157 |
| B | TRP199 |
| B | ARG200 |
| B | TYR217 |
| B | TYR296 |
| B | HOH624 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP C 502 |
| Chain | Residue |
| B | VAL10 |
| B | PRO11 |
| B | THR13 |
| B | PRO14 |
| B | ALA15 |
| B | GLY16 |
| B | ARG17 |
| C | GLY38 |
| C | LEU39 |
| C | GLY40 |
| C | LYS41 |
| C | TYR42 |
| C | SER64 |
| C | GLY65 |
| C | LYS69 |
| C | TYR87 |
| C | ILE105 |
| C | LEU106 |
| C | PRO107 |
| C | ASN108 |
| C | LEU110 |
| C | HIS111 |
| C | GLU128 |
| C | LYS129 |
| C | ARG157 |
| C | ALA196 |
| C | TRP199 |
| C | ARG200 |
| C | ASP213 |
| C | TYR217 |
| C | TYR296 |
| C | HOH509 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NDP D 503 |
| Chain | Residue |
| D | PRO107 |
| D | ASN108 |
| D | HIS111 |
| D | GLU128 |
| D | LYS129 |
| D | GLY155 |
| D | ARG157 |
| D | TRP199 |
| D | ARG200 |
| D | TYR217 |
| D | GOL602 |
| D | HOH604 |
| D | HOH653 |
| D | HOH678 |
| D | HOH679 |
| D | LEU39 |
| D | GLY40 |
| D | LYS41 |
| D | TYR42 |
| D | SER64 |
| D | GLY65 |
| D | LYS69 |
| D | TYR87 |
| D | ILE105 |
| D | LEU106 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 604 |
| Chain | Residue |
| A | SER272 |
| B | GLY180 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 601 |
| Chain | Residue |
| A | GLY366 |
| B | ARG234 |
| B | PRO368 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 602 |
| Chain | Residue |
| D | LYS129 |
| D | ARG200 |
| D | ASP213 |
| D | TYR217 |
| D | NDP503 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 603 |
| Chain | Residue |
| A | SER239 |
| A | PHE246 |
| A | VAL249 |
| A | HOH638 |
| A | HOH679 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ofg |
| Chain | Residue | Details |
| A | LYS129 | |
| A | TYR217 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ofg |
| Chain | Residue | Details |
| B | LYS129 | |
| B | TYR217 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ofg |
| Chain | Residue | Details |
| C | LYS129 | |
| C | TYR217 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ofg |
| Chain | Residue | Details |
| D | LYS129 | |
| D | TYR217 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 868 |
| Chain | Residue | Details |
| A | LYS129 | electrostatic stabiliser |
| A | TYR217 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 868 |
| Chain | Residue | Details |
| B | LYS129 | electrostatic stabiliser |
| B | TYR217 | proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 868 |
| Chain | Residue | Details |
| C | LYS129 | electrostatic stabiliser |
| C | TYR217 | proton shuttle (general acid/base) |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 868 |
| Chain | Residue | Details |
| D | LYS129 | electrostatic stabiliser |
| D | TYR217 | proton shuttle (general acid/base) |
