1OFG
GLUCOSE-FRUCTOSE OXIDOREDUCTASE
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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0006061 | biological_process | sorbitol biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0047061 | molecular_function | glucose-fructose oxidoreductase activity |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0006061 | biological_process | sorbitol biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0047061 | molecular_function | glucose-fructose oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NDP A 500 |
| Chain | Residue |
| A | GLY38 |
| A | ILE105 |
| A | LEU106 |
| A | PRO107 |
| A | ASN108 |
| A | LEU110 |
| A | HIS111 |
| A | GLU128 |
| A | LYS129 |
| A | GLY155 |
| A | ARG157 |
| A | LEU39 |
| A | ALA196 |
| A | TRP199 |
| A | ARG200 |
| A | TYR217 |
| A | TYR296 |
| A | HOH501 |
| A | HOH505 |
| A | HOH514 |
| A | HOH517 |
| A | HOH522 |
| A | GLY40 |
| A | HOH546 |
| A | HOH598 |
| A | HOH599 |
| D | VAL10 |
| 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 | 39 |
| Details | BINDING SITE FOR RESIDUE NDP B 500 |
| Chain | Residue |
| B | GLY38 |
| 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 | GLY155 |
| B | ARG157 |
| B | ALA196 |
| B | TRP199 |
| B | ARG200 |
| B | TYR217 |
| B | TYR296 |
| B | HOH508 |
| B | HOH513 |
| B | HOH521 |
| B | HOH524 |
| B | HOH529 |
| B | HOH554 |
| B | HOH606 |
| B | HOH607 |
| C | VAL10 |
| C | PRO11 |
| C | THR13 |
| C | PRO14 |
| C | ALA15 |
| C | GLY16 |
| C | ARG17 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NDP C 500 |
| Chain | Residue |
| C | HIS111 |
| C | GLU128 |
| C | LYS129 |
| C | GLY155 |
| C | ARG157 |
| C | ALA196 |
| C | TRP199 |
| C | ARG200 |
| C | TYR217 |
| C | TYR296 |
| C | HOH518 |
| C | HOH523 |
| C | HOH531 |
| C | HOH534 |
| C | HOH539 |
| C | HOH564 |
| C | HOH615 |
| C | HOH616 |
| 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 |
| site_id | AC4 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NDP D 500 |
| Chain | Residue |
| A | VAL10 |
| A | PRO11 |
| A | THR13 |
| A | PRO14 |
| A | ALA15 |
| A | GLY16 |
| A | ARG17 |
| D | GLY38 |
| D | LEU39 |
| D | GLY40 |
| D | LYS41 |
| D | TYR42 |
| D | SER64 |
| D | GLY65 |
| D | LYS69 |
| D | TYR87 |
| D | ILE105 |
| D | LEU106 |
| D | PRO107 |
| D | ASN108 |
| D | LEU110 |
| D | HIS111 |
| D | GLU128 |
| D | LYS129 |
| D | GLY155 |
| D | ARG157 |
| D | ALA196 |
| D | TRP199 |
| D | ARG200 |
| D | TYR217 |
| D | TYR296 |
| D | HOH526 |
| D | HOH530 |
| D | HOH539 |
| D | HOH542 |
| D | HOH547 |
| D | HOH571 |
| D | HOH622 |
| D | HOH623 |
| site_id | AC5 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NDP E 500 |
| Chain | Residue |
| E | VAL10 |
| E | PRO11 |
| E | THR13 |
| E | PRO14 |
| E | ALA15 |
| E | GLY16 |
| E | ARG17 |
| E | GLY38 |
| E | LEU39 |
| E | GLY40 |
| E | LYS41 |
| E | TYR42 |
| E | SER64 |
| E | GLY65 |
| E | LYS69 |
| E | TYR87 |
| E | ILE105 |
| E | LEU106 |
| E | PRO107 |
| E | ASN108 |
| E | LEU110 |
| E | HIS111 |
| E | GLU128 |
| E | LYS129 |
| E | GLY155 |
| E | ARG157 |
| E | ALA196 |
| E | TRP199 |
| E | ARG200 |
| E | TYR217 |
| E | TYR296 |
| E | HOH561 |
| E | HOH566 |
| E | HOH575 |
| E | HOH578 |
| E | HOH583 |
| E | HOH620 |
| E | HOH683 |
| E | HOH684 |
| site_id | AC6 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NDP F 500 |
| Chain | Residue |
| F | VAL10 |
| F | PRO11 |
| F | THR13 |
| F | PRO14 |
| F | ALA15 |
| F | GLY16 |
| F | ARG17 |
| F | GLY38 |
| F | LEU39 |
| F | GLY40 |
| F | LYS41 |
| F | TYR42 |
| F | SER64 |
| F | GLY65 |
| F | LYS69 |
| F | TYR87 |
| F | ILE105 |
| F | LEU106 |
| F | PRO107 |
| F | ASN108 |
| F | LEU110 |
| F | HIS111 |
| F | GLU128 |
| F | LYS129 |
| F | GLY155 |
| F | ARG157 |
| F | ALA196 |
| F | TRP199 |
| F | ARG200 |
| F | TYR217 |
| F | TYR296 |
| F | HOH701 |
| F | HOH706 |
| F | HOH715 |
| F | HOH718 |
| F | HOH723 |
| F | HOH760 |
| F | HOH823 |
| F | HOH824 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8994968 |
| Chain | Residue | Details |
| A | LYS129 | |
| A | TYR217 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8994968 |
| Chain | Residue | Details |
| B | LYS129 | |
| B | TYR217 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8994968 |
| Chain | Residue | Details |
| C | LYS129 | |
| C | TYR217 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8994968 |
| Chain | Residue | Details |
| D | LYS129 | |
| D | TYR217 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8994968 |
| Chain | Residue | Details |
| E | LYS129 | |
| E | TYR217 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8994968 |
| Chain | Residue | Details |
| F | LYS129 | |
| F | 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) |
| site_id | MCSA5 |
| Number of Residues | 2 |
| Details | M-CSA 868 |
| Chain | Residue | Details |
| E | LYS129 | electrostatic stabiliser |
| E | TYR217 | proton shuttle (general acid/base) |
| site_id | MCSA6 |
| Number of Residues | 2 |
| Details | M-CSA 868 |
| Chain | Residue | Details |
| F | LYS129 | electrostatic stabiliser |
| F | TYR217 | proton shuttle (general acid/base) |
