3BG6
Pyranose 2-oxidase from Trametes multicolor, E542K 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 | ASN593 |
| A | THR595 |
| A | HOH809 |
| A | HOH811 |
| A | HOH836 |
| A | GLY55 |
| A | HOH843 |
| A | HOH858 |
| A | HOH861 |
| A | HOH887 |
| A | HOH897 |
| A | HOH1010 |
| A | HOH1029 |
| A | PRO56 |
| A | ILE57 |
| A | ASP76 |
| A | ILE77 |
| A | THR158 |
| A | ARG159 |
| site_id | AC2 |
| Number of Residues | 36 |
| 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 | SER165 |
| B | HIS167 |
| B | TRP168 |
| B | THR169 |
| B | CYS170 |
| B | ALA171 |
| B | VAL281 |
| B | CYS283 |
| B | THR319 |
| B | ALA320 |
| B | HIS324 |
| B | LEU547 |
| B | ASN593 |
| B | THR595 |
| B | HOH806 |
| B | HOH814 |
| B | HOH817 |
| B | HOH863 |
| B | HOH901 |
| B | HOH916 |
| B | HOH925 |
| B | HOH927 |
| B | HOH1016 |
| B | HOH1110 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD C 801 |
| Chain | Residue |
| C | HOH832 |
| C | HOH838 |
| C | HOH845 |
| C | HOH860 |
| C | HOH866 |
| C | HOH885 |
| C | HOH939 |
| C | HOH955 |
| C | HOH1059 |
| C | VAL52 |
| 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 | ASN593 |
| C | THR595 |
| C | HOH810 |
| site_id | AC4 |
| Number of Residues | 36 |
| 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 | SER165 |
| D | HIS167 |
| D | TRP168 |
| D | THR169 |
| D | CYS170 |
| D | ALA171 |
| D | VAL281 |
| D | CYS283 |
| D | THR319 |
| D | ALA320 |
| D | HIS324 |
| D | LEU547 |
| D | ASN593 |
| D | THR595 |
| D | HOH935 |
| D | HOH944 |
| D | HOH966 |
| D | HOH975 |
| D | HOH976 |
| D | HOH984 |
| D | HOH1049 |
| D | HOH1061 |
| D | HOH1137 |
| D | HOH1148 |
| site_id | AC5 |
| Number of Residues | 35 |
| 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 | SER165 |
| E | HIS167 |
| E | TRP168 |
| E | THR169 |
| E | CYS170 |
| E | ALA171 |
| E | VAL281 |
| E | CYS283 |
| E | THR319 |
| E | ALA320 |
| E | HIS324 |
| E | LEU547 |
| E | ASN593 |
| E | THR595 |
| E | HOH1116 |
| E | HOH1153 |
| E | HOH1171 |
| E | HOH1173 |
| E | HOH1174 |
| E | HOH1188 |
| E | HOH1189 |
| E | HOH1191 |
| E | HOH1321 |
| 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 | ASN593 |
| F | THR595 |
| F | HOH808 |
| F | HOH846 |
| F | HOH856 |
| F | HOH859 |
| F | HOH880 |
| F | HOH890 |
| F | HOH905 |
| F | HOH919 |
| F | HOH949 |
| F | HOH989 |
| site_id | AC7 |
| Number of Residues | 37 |
| 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 | SER165 |
| G | HIS167 |
| G | TRP168 |
| G | THR169 |
| G | CYS170 |
| G | ALA171 |
| G | VAL281 |
| G | CYS283 |
| G | THR319 |
| G | ALA320 |
| G | HIS324 |
| G | LEU547 |
| G | ASN593 |
| G | THR595 |
| G | HOH805 |
| G | HOH810 |
| G | HOH826 |
| G | HOH838 |
| G | HOH844 |
| G | HOH864 |
| G | HOH872 |
| G | HOH892 |
| G | HOH1033 |
| G | HOH1037 |
| G | HOH1112 |
| 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 | ASN593 |
| H | THR595 |
| H | HOH816 |
| H | HOH824 |
| H | HOH829 |
| H | HOH859 |
| H | HOH867 |
| H | HOH881 |
| H | HOH928 |
| H | HOH1075 |
| H | HOH1078 |
| H | HOH1112 |
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 |
