3BG7
Pyranose 2-oxidase from Trametes multicolor, L537G mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050233 | molecular_function | pyranose oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050233 | molecular_function | pyranose oxidase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0050233 | molecular_function | pyranose oxidase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0050233 | molecular_function | pyranose oxidase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0050233 | molecular_function | pyranose oxidase activity |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0050233 | molecular_function | pyranose oxidase activity |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| G | 0042597 | cellular_component | periplasmic space |
| G | 0050233 | molecular_function | pyranose oxidase activity |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| H | 0042597 | cellular_component | periplasmic space |
| H | 0050233 | molecular_function | pyranose oxidase activity |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD A 801 |
| Chain | Residue |
| A | VAL52 |
| A | VAL160 |
| A | GLY163 |
| A | MET164 |
| A | SER165 |
| A | HIS167 |
| A | TRP168 |
| A | THR169 |
| A | CYS170 |
| A | ALA171 |
| A | VAL281 |
| A | GLY53 |
| A | CYS283 |
| A | THR319 |
| A | ALA320 |
| A | HIS324 |
| A | LEU547 |
| A | HIS548 |
| A | ASN593 |
| A | THR595 |
| A | HOH811 |
| A | HOH812 |
| A | GLY55 |
| A | HOH835 |
| A | HOH840 |
| A | HOH871 |
| A | HOH888 |
| A | HOH937 |
| A | HOH1006 |
| A | HOH1057 |
| A | PRO56 |
| A | ILE57 |
| A | ASP76 |
| A | ILE77 |
| A | THR158 |
| A | ARG159 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD B 801 |
| Chain | Residue |
| B | VAL52 |
| B | GLY53 |
| B | GLY55 |
| B | PRO56 |
| B | ILE57 |
| B | ASP76 |
| B | ILE77 |
| B | THR158 |
| B | ARG159 |
| B | VAL160 |
| B | GLY163 |
| B | MET164 |
| B | HIS167 |
| B | TRP168 |
| B | THR169 |
| B | CYS170 |
| B | ALA171 |
| B | VAL281 |
| B | CYS283 |
| B | THR319 |
| B | ALA320 |
| B | HIS324 |
| B | LEU547 |
| B | HIS548 |
| B | ASN593 |
| B | THR595 |
| B | HOH805 |
| B | HOH817 |
| B | HOH830 |
| B | HOH858 |
| B | HOH902 |
| B | HOH909 |
| B | HOH938 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD C 801 |
| Chain | Residue |
| C | HOH856 |
| C | HOH891 |
| C | HOH958 |
| C | GLY53 |
| C | GLY55 |
| C | PRO56 |
| C | ILE57 |
| C | ASP76 |
| C | ILE77 |
| C | THR158 |
| C | ARG159 |
| C | VAL160 |
| C | GLY163 |
| C | MET164 |
| C | SER165 |
| C | HIS167 |
| C | TRP168 |
| C | THR169 |
| C | CYS170 |
| C | ALA171 |
| C | VAL281 |
| C | CYS283 |
| C | THR319 |
| C | ALA320 |
| C | HIS324 |
| C | LEU547 |
| C | HIS548 |
| C | ASN593 |
| C | THR595 |
| C | HOH806 |
| C | HOH835 |
| C | HOH840 |
| C | HOH851 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD D 801 |
| Chain | Residue |
| D | VAL52 |
| D | GLY53 |
| D | GLY55 |
| D | PRO56 |
| D | ILE57 |
| D | ASP76 |
| D | ILE77 |
| D | THR158 |
| D | ARG159 |
| D | VAL160 |
| D | GLY163 |
| D | MET164 |
| D | HIS167 |
| D | TRP168 |
| D | THR169 |
| D | CYS170 |
| D | ALA171 |
| D | VAL281 |
| D | CYS283 |
| D | THR319 |
| D | ALA320 |
| D | HIS324 |
| D | LEU547 |
| D | HIS548 |
| D | ASN593 |
| D | THR595 |
| D | HOH810 |
| D | HOH816 |
| D | HOH822 |
| D | HOH877 |
| D | HOH892 |
| D | HOH944 |
| D | HOH990 |
| D | HOH996 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD E 801 |
| Chain | Residue |
| E | VAL52 |
| E | GLY53 |
| E | GLY55 |
| E | PRO56 |
| E | ILE57 |
| E | ASP76 |
| E | ILE77 |
| E | THR158 |
| E | ARG159 |
| E | VAL160 |
| E | GLY163 |
| E | MET164 |
| E | HIS167 |
| E | TRP168 |
| E | THR169 |
| E | CYS170 |
| E | ALA171 |
| E | VAL281 |
| E | CYS283 |
| E | THR319 |
| E | ALA320 |
| E | HIS324 |
| E | LEU547 |
| E | HIS548 |
| E | ASN593 |
| E | THR595 |
| E | HOH807 |
| E | HOH852 |
| E | HOH862 |
| E | HOH867 |
| E | HOH868 |
| E | HOH883 |
| E | HOH929 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD F 801 |
| Chain | Residue |
| F | VAL52 |
| F | GLY53 |
| F | GLY55 |
| F | PRO56 |
| F | ILE57 |
| F | ASP76 |
| F | ILE77 |
| F | THR158 |
| F | ARG159 |
| F | VAL160 |
| F | GLY163 |
| F | MET164 |
| F | SER165 |
| F | HIS167 |
| F | TRP168 |
| F | THR169 |
| F | CYS170 |
| F | ALA171 |
| F | VAL281 |
| F | CYS283 |
| F | THR319 |
| F | ALA320 |
| F | HIS324 |
| F | LEU547 |
| F | HIS548 |
| F | ASN593 |
| F | THR595 |
| F | HOH808 |
| F | HOH843 |
| F | HOH871 |
| F | HOH873 |
| F | HOH879 |
| F | HOH888 |
| F | HOH893 |
| F | HOH937 |
| F | HOH992 |
| site_id | AC7 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD G 801 |
| Chain | Residue |
| G | VAL52 |
| G | GLY53 |
| G | GLY55 |
| G | PRO56 |
| G | ILE57 |
| G | ASP76 |
| G | ILE77 |
| G | THR158 |
| G | ARG159 |
| G | VAL160 |
| G | GLY163 |
| G | MET164 |
| G | HIS167 |
| G | TRP168 |
| G | THR169 |
| G | CYS170 |
| G | ALA171 |
| G | VAL281 |
| G | CYS283 |
| G | THR319 |
| G | ALA320 |
| G | HIS324 |
| G | LEU547 |
| G | HIS548 |
| G | CYS583 |
| G | ASN593 |
| G | THR595 |
| G | HOH928 |
| G | HOH932 |
| G | HOH933 |
| G | HOH949 |
| G | HOH956 |
| G | HOH993 |
| G | HOH1024 |
| G | HOH1049 |
| site_id | AC8 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD H 801 |
| Chain | Residue |
| H | VAL52 |
| H | GLY53 |
| H | GLY55 |
| H | PRO56 |
| H | ILE57 |
| H | ASP76 |
| H | ILE77 |
| H | THR158 |
| H | ARG159 |
| H | VAL160 |
| H | GLY163 |
| H | MET164 |
| H | SER165 |
| H | HIS167 |
| H | TRP168 |
| H | THR169 |
| H | CYS170 |
| H | ALA171 |
| H | VAL281 |
| H | CYS283 |
| H | THR319 |
| H | ALA320 |
| H | HIS324 |
| H | LEU547 |
| H | HIS548 |
| H | ASN593 |
| H | THR595 |
| H | HOH813 |
| H | HOH825 |
| H | HOH828 |
| H | HOH851 |
| H | HOH858 |
| H | HOH882 |
| H | HOH996 |
| H | HOH1015 |
| H | HOH1041 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| A | ASN593 | |
| A | HIS548 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| B | ASN593 | |
| B | HIS548 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| C | ASN593 | |
| C | HIS548 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| D | ASN593 | |
| D | HIS548 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| E | ASN593 | |
| E | HIS548 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| F | ASN593 | |
| F | HIS548 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| G | ASN593 | |
| G | HIS548 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| H | ASN593 | |
| H | HIS548 |
