2IGN
Crystal structure of recombinant pyranose 2-oxidase H167A 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 7001 |
| Chain | Residue |
| A | VAL52 |
| A | VAL160 |
| A | GLY163 |
| A | MET164 |
| A | ALA167 |
| 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 | HOH8006 |
| A | HOH8007 |
| A | HOH8012 |
| A | HOH8018 |
| A | GLY55 |
| A | HOH8037 |
| A | HOH8050 |
| A | HOH8064 |
| A | HOH8077 |
| A | HOH8088 |
| A | HOH8107 |
| A | HOH8347 |
| A | PRO56 |
| A | ILE57 |
| A | ASP76 |
| A | ILE77 |
| A | THR158 |
| A | ARG159 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD B 7002 |
| 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 | TRP168 |
| B | THR169 |
| B | CYS170 |
| B | ALA171 |
| B | VAL281 |
| B | CYS283 |
| B | THR319 |
| B | ALA320 |
| B | HIS324 |
| B | LEU547 |
| B | ASN593 |
| B | THR595 |
| B | HOH8007 |
| B | HOH8012 |
| B | HOH8035 |
| B | HOH8037 |
| B | HOH8061 |
| B | HOH8071 |
| B | HOH8076 |
| B | HOH8093 |
| B | HOH8141 |
| B | HOH8206 |
| B | HOH8639 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD D 7003 |
| Chain | Residue |
| D | HOH8074 |
| D | HOH8102 |
| D | HOH8103 |
| D | HOH8107 |
| D | HOH8111 |
| D | HOH8124 |
| D | HOH8150 |
| 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 | ALA167 |
| 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 | HOH8012 |
| D | HOH8017 |
| D | HOH8030 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD C 7004 |
| 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 | ALA167 |
| 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 | HOH8024 |
| C | HOH8025 |
| C | HOH8036 |
| C | HOH8046 |
| C | HOH8066 |
| C | HOH8069 |
| C | HOH8106 |
| C | HOH8117 |
| C | HOH8119 |
| C | HOH8176 |
| C | HOH8210 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD E 7005 |
| 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 | TRP168 |
| E | THR169 |
| E | CYS170 |
| E | ALA171 |
| E | VAL281 |
| E | CYS283 |
| E | THR319 |
| E | ALA320 |
| E | HIS324 |
| E | LEU547 |
| E | ASN593 |
| E | THR595 |
| E | HOH8012 |
| E | HOH8018 |
| E | HOH8034 |
| E | HOH8037 |
| E | HOH8072 |
| E | HOH8105 |
| E | HOH8106 |
| E | HOH8122 |
| E | HOH8160 |
| E | HOH8211 |
| E | HOH8269 |
| site_id | AC6 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD F 7006 |
| 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 | TRP168 |
| F | THR169 |
| F | CYS170 |
| F | ALA171 |
| F | VAL281 |
| F | CYS283 |
| F | THR319 |
| F | ALA320 |
| F | HIS324 |
| F | LEU547 |
| F | ASN593 |
| F | THR595 |
| F | HOH8008 |
| F | HOH8029 |
| F | HOH8039 |
| F | HOH8051 |
| F | HOH8054 |
| F | HOH8058 |
| F | HOH8075 |
| F | HOH8098 |
| F | HOH8112 |
| F | HOH8129 |
| F | HOH8155 |
| site_id | AC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD H 7007 |
| 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 | ALA167 |
| 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 | HOH8006 |
| H | HOH8020 |
| H | HOH8027 |
| H | HOH8038 |
| H | HOH8041 |
| H | HOH8065 |
| H | HOH8104 |
| H | HOH8171 |
| H | HOH8173 |
| H | HOH8176 |
| H | HOH8198 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD G 7008 |
| Chain | Residue |
| G | GLY53 |
| G | GLY55 |
| G | PRO56 |
| G | ILE57 |
| G | ASP76 |
| G | ILE77 |
| G | THR158 |
| G | ARG159 |
| G | VAL160 |
| G | GLY163 |
| G | MET164 |
| 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 | HOH8009 |
| G | HOH8012 |
| G | HOH8028 |
| G | HOH8030 |
| G | HOH8066 |
| G | HOH8111 |
| G | HOH8123 |
| G | HOH8140 |
| G | HOH8151 |
| G | HOH8187 |
| G | HOH8228 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MES F 8001 |
| Chain | Residue |
| E | SER462 |
| E | ILE463 |
| E | ASP464 |
| F | LEU121 |
| F | VAL122 |
| F | VAL123 |
| F | TRP131 |
| F | GLN132 |
| F | ALA133 |
| F | PHE137 |
| F | ARG139 |
| F | HOH8407 |
| G | LEU149 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MES A 8002 |
| Chain | Residue |
| A | LEU121 |
| A | VAL122 |
| A | VAL123 |
| A | TRP131 |
| A | GLN132 |
| A | ALA133 |
| A | PHE137 |
| A | ARG139 |
| A | HOH8414 |
| A | HOH8633 |
| B | SER462 |
| B | ILE463 |
| B | ASP464 |
| D | LEU149 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MES B 8003 |
| Chain | Residue |
| A | SER462 |
| A | ILE463 |
| A | ASP464 |
| B | LEU121 |
| B | VAL122 |
| B | VAL123 |
| B | TRP131 |
| B | GLN132 |
| B | ALA133 |
| B | PHE137 |
| B | ARG139 |
| B | HOH8503 |
| B | HOH8607 |
| C | LEU149 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MES H 8004 |
| Chain | Residue |
| E | LEU149 |
| G | SER462 |
| G | ILE463 |
| G | ASP464 |
| H | LEU121 |
| H | VAL123 |
| H | TRP131 |
| H | GLN132 |
| H | ALA133 |
| H | PHE137 |
| H | ARG139 |
| H | HOH8306 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MES D 8005 |
| 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 | HOH8310 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MES G 8006 |
| Chain | Residue |
| F | LEU149 |
| G | LEU121 |
| G | VAL122 |
| G | VAL123 |
| G | TRP131 |
| G | GLN132 |
| G | ALA133 |
| G | PHE137 |
| G | ARG139 |
| G | HOH8371 |
| H | SER462 |
| H | ILE463 |
| H | ASP464 |
| site_id | BC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MES E 8007 |
| Chain | Residue |
| E | LEU121 |
| E | VAL122 |
| E | VAL123 |
| E | TRP131 |
| E | GLN132 |
| E | ALA133 |
| E | PHE136 |
| E | PHE137 |
| E | ARG139 |
| E | HOH8255 |
| E | HOH8344 |
| F | SER462 |
| F | ILE463 |
| F | ASP464 |
| F | HOH8327 |
| H | LEU149 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MES C 8008 |
| Chain | Residue |
| B | LEU149 |
| C | LEU121 |
| C | VAL122 |
| C | VAL123 |
| C | TRP131 |
| C | GLN132 |
| C | ALA133 |
| C | PHE137 |
| C | ARG139 |
| C | HOH8251 |
| D | SER462 |
| D | ILE463 |
| D | ASP464 |
| D | HOH8439 |
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 |
| D | ASN593 | |
| D | HIS548 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| C | ASN593 | |
| C | 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 |
| H | ASN593 | |
| H | HIS548 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kdg |
| Chain | Residue | Details |
| G | ASN593 | |
| G | HIS548 |






