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) |