1EVJ
CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D
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 | 23 |
| Details | BINDING SITE FOR RESIDUE NAD A 500 |
| Chain | Residue |
| A | GLY38 |
| A | PRO107 |
| A | ASN108 |
| A | HIS111 |
| A | GLU128 |
| A | LYS129 |
| A | ARG157 |
| A | TRP199 |
| A | ARG200 |
| A | TYR217 |
| A | TYR296 |
| A | LEU39 |
| A | HOH605 |
| A | HOH647 |
| A | HOH656 |
| A | HOH657 |
| A | GLY40 |
| A | LYS41 |
| A | TYR42 |
| A | ASP64 |
| A | TYR87 |
| A | ILE105 |
| A | LEU106 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | GLY38 |
| B | LEU39 |
| B | GLY40 |
| B | LYS41 |
| B | TYR42 |
| B | ASP64 |
| B | TYR87 |
| B | ILE105 |
| B | LEU106 |
| B | PRO107 |
| B | ASN108 |
| B | HIS111 |
| B | GLU128 |
| B | LYS129 |
| B | ARG157 |
| B | TRP199 |
| B | ARG200 |
| B | TYR217 |
| B | TYR296 |
| B | HOH600 |
| B | HOH638 |
| B | HOH675 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD C 502 |
| Chain | Residue |
| C | GLY38 |
| C | LEU39 |
| C | GLY40 |
| C | LYS41 |
| C | TYR42 |
| C | ASP64 |
| C | TYR87 |
| C | ILE105 |
| C | LEU106 |
| C | PRO107 |
| C | ASN108 |
| C | HIS111 |
| C | GLU128 |
| C | LYS129 |
| C | ARG157 |
| C | TRP199 |
| C | ARG200 |
| C | TYR217 |
| C | TYR296 |
| C | HOH601 |
| C | HOH658 |
| C | HOH659 |
| C | HOH706 |
| C | HOH728 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD D 503 |
| Chain | Residue |
| D | GLY38 |
| D | LEU39 |
| D | GLY40 |
| D | LYS41 |
| D | TYR42 |
| D | ASP64 |
| D | TYR87 |
| D | ILE105 |
| D | LEU106 |
| D | PRO107 |
| D | ASN108 |
| D | HIS111 |
| D | GLU128 |
| D | LYS129 |
| D | ARG157 |
| D | TRP199 |
| D | ARG200 |
| D | TYR217 |
| D | TYR296 |
| D | HOH651 |
| D | HOH652 |
| D | HOH661 |
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) |
