2IGM
Crystal structure of recombinant pyranose 2-oxidase H548N 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 | 35 |
| Details | BINDING SITE FOR RESIDUE FAD A 801 |
| Chain | Residue |
| A | VAL52 |
| A | VAL160 |
| A | GLY163 |
| A | MET164 |
| A | HIS167 |
| A | TRP168 |
| A | THR169 |
| A | CYS170 |
| A | ALA171 |
| A | VAL281 |
| A | CYS283 |
| A | GLY53 |
| A | THR319 |
| A | ALA320 |
| A | HIS324 |
| A | LEU547 |
| A | ASN593 |
| A | THR595 |
| A | HOH7023 |
| A | HOH7038 |
| A | HOH7045 |
| A | HOH7059 |
| A | GLY55 |
| A | HOH7075 |
| A | HOH7085 |
| A | HOH7089 |
| A | HOH7118 |
| A | HOH7150 |
| A | HOH7161 |
| A | PRO56 |
| A | ILE57 |
| A | ASP76 |
| A | ILE77 |
| A | THR158 |
| A | ARG159 |
| site_id | AC2 |
| Number of Residues | 37 |
| 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 | ILE107 |
| 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 | HOH7011 |
| B | HOH7027 |
| B | HOH7100 |
| B | HOH7104 |
| B | HOH7110 |
| B | HOH7113 |
| B | HOH7134 |
| B | HOH7140 |
| B | HOH7141 |
| B | HOH7222 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD D 801 |
| Chain | Residue |
| D | HOH7032 |
| D | HOH7039 |
| D | HOH7042 |
| D | HOH7078 |
| D | HOH7088 |
| D | HOH7105 |
| D | HOH7109 |
| D | HOH7140 |
| D | HOH7147 |
| 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 | ASN593 |
| D | THR595 |
| D | HOH7021 |
| D | HOH7031 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD C 801 |
| Chain | Residue |
| 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 | 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 | HOH7024 |
| C | HOH7028 |
| C | HOH7041 |
| C | HOH7061 |
| C | HOH7066 |
| C | HOH7072 |
| C | HOH7092 |
| C | HOH7140 |
| C | HOH7159 |
| C | HOH7165 |
| C | HOH7176 |
| 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 | 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 | HOH7006 |
| E | HOH7036 |
| E | HOH7052 |
| E | HOH7055 |
| E | HOH7066 |
| E | HOH7072 |
| E | HOH7096 |
| E | HOH7116 |
| E | HOH7262 |
| E | HOH7294 |
| site_id | AC6 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD F 801 |
| Chain | Residue |
| F | GLY53 |
| F | GLY55 |
| F | PRO56 |
| F | ILE57 |
| F | ASP76 |
| F | ILE77 |
| F | THR158 |
| F | ARG159 |
| F | VAL160 |
| F | GLY163 |
| F | MET164 |
| 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 | HOH7008 |
| F | HOH7020 |
| F | HOH7036 |
| F | HOH7053 |
| F | HOH7060 |
| F | HOH7065 |
| F | HOH7091 |
| F | HOH7119 |
| F | HOH7129 |
| F | HOH7156 |
| site_id | AC7 |
| Number of Residues | 38 |
| 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 | ILE107 |
| 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 | HOH7011 |
| G | HOH7016 |
| G | HOH7029 |
| G | HOH7033 |
| G | HOH7039 |
| G | HOH7081 |
| G | HOH7136 |
| G | HOH7138 |
| G | HOH7147 |
| G | HOH7162 |
| G | HOH7308 |
| site_id | AC8 |
| Number of Residues | 38 |
| 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 | ILE107 |
| 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 | HOH7007 |
| H | HOH7014 |
| H | HOH7026 |
| H | HOH7028 |
| H | HOH7042 |
| H | HOH7052 |
| H | HOH7075 |
| H | HOH7117 |
| H | HOH7152 |
| H | HOH7157 |
| H | HOH7209 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MES F 7001 |
| Chain | Residue |
| E | SER462 |
| E | ILE463 |
| E | ASP464 |
| F | LEU121 |
| F | VAL123 |
| F | TRP131 |
| F | GLN132 |
| F | ALA133 |
| F | THR135 |
| F | PHE137 |
| F | ARG139 |
| G | LEU149 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MES H 7002 |
| Chain | Residue |
| E | LEU149 |
| G | SER462 |
| G | ILE463 |
| G | ASP464 |
| H | LEU121 |
| H | VAL122 |
| H | VAL123 |
| H | TRP131 |
| H | GLN132 |
| H | ALA133 |
| H | PHE137 |
| H | ARG139 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MES A 7003 |
| Chain | Residue |
| A | LEU121 |
| A | VAL122 |
| A | VAL123 |
| A | TRP131 |
| A | GLN132 |
| A | ALA133 |
| A | PHE137 |
| A | ARG139 |
| B | SER462 |
| B | ILE463 |
| B | ASP464 |
| D | LEU149 |
| site_id | BC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MES E 7004 |
| Chain | Residue |
| E | LEU121 |
| E | VAL122 |
| E | VAL123 |
| E | TRP131 |
| E | GLN132 |
| E | ALA133 |
| E | PHE137 |
| E | ARG139 |
| E | HOH7426 |
| E | HOH7440 |
| F | SER462 |
| F | ILE463 |
| F | ASP464 |
| H | LEU149 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MES C 7005 |
| Chain | Residue |
| B | LEU149 |
| C | LEU121 |
| C | VAL123 |
| C | TRP131 |
| C | GLN132 |
| C | ALA133 |
| C | PHE137 |
| C | ARG139 |
| D | SER462 |
| D | ILE463 |
| D | ASP464 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MES B 7006 |
| Chain | Residue |
| A | SER462 |
| A | ILE463 |
| A | ASP464 |
| B | LEU121 |
| B | VAL122 |
| B | VAL123 |
| B | TRP131 |
| B | GLN132 |
| B | ALA133 |
| B | PHE137 |
| B | ARG139 |
| C | LEU149 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MES D 7007 |
| Chain | Residue |
| A | LEU149 |
| C | SER462 |
| C | ILE463 |
| C | ASP464 |
| D | LEU121 |
| D | VAL122 |
| D | VAL123 |
| D | TRP131 |
| D | GLN132 |
| D | ALA133 |
| D | PHE137 |
| D | ARG139 |
| D | HOH7447 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MES G 7008 |
| Chain | Residue |
| F | LEU149 |
| G | LEU121 |
| G | VAL123 |
| G | TRP131 |
| G | GLN132 |
| G | ALA133 |
| G | PHE137 |
| G | ARG139 |
| H | SER462 |
| H | ILE463 |
| H | ASP464 |
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 | HIS553 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| B | ASN593 | |
| B | HIS553 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| D | ASN593 | |
| D | HIS553 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| C | ASN593 | |
| C | HIS553 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| E | ASN593 | |
| E | HIS553 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| F | ASN593 | |
| F | HIS553 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| G | ASN593 | |
| G | HIS553 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| H | ASN593 | |
| H | HIS553 |






