4MOK
Pyranose 2-oxidase H167A mutant soaked with 3-fluorinated galactose (not bound)
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 |
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 | TRP168 |
A | THR169 |
A | CYS170 |
A | ALA171 |
A | VAL281 |
A | CYS283 |
A | THR319 |
A | GLY53 |
A | ALA320 |
A | HIS324 |
A | LEU547 |
A | ASN593 |
A | PRO594 |
A | THR595 |
A | HOH926 |
A | HOH938 |
A | HOH945 |
A | HOH962 |
A | GLY55 |
A | HOH976 |
A | HOH1019 |
A | HOH1054 |
A | HOH1057 |
A | HOH1144 |
A | HOH1145 |
A | PRO56 |
A | ILE57 |
A | ASP76 |
A | ILE77 |
A | THR158 |
A | ARG159 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 12P A 802 |
Chain | Residue |
A | PRO144 |
A | GLN146 |
A | ASP147 |
A | PRO148 |
A | HOH1138 |
A | HOH1339 |
D | SER134 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE MES A 803 |
Chain | Residue |
A | LEU121 |
A | VAL123 |
A | TRP131 |
A | ALA133 |
A | THR135 |
A | PHE137 |
A | ARG139 |
A | HOH1092 |
A | HOH1216 |
B | SER462 |
B | ILE463 |
B | ASP464 |
D | LEU149 |
site_id | AC4 |
Number of Residues | 35 |
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 | TRP168 |
B | THR169 |
B | CYS170 |
B | ALA171 |
B | VAL281 |
B | CYS283 |
B | THR319 |
B | ALA320 |
B | HIS324 |
B | LEU547 |
B | ASN593 |
B | THR595 |
B | HOH925 |
B | HOH964 |
B | HOH990 |
B | HOH992 |
B | HOH1002 |
B | HOH1016 |
B | HOH1024 |
B | HOH1052 |
B | HOH1078 |
B | HOH1123 |
B | HOH1352 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 12P B 802 |
Chain | Residue |
B | PRO144 |
B | ASP147 |
B | PRO148 |
B | HOH1274 |
B | HOH1285 |
C | SER134 |
site_id | AC6 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD C 801 |
Chain | Residue |
C | PRO56 |
C | ILE57 |
C | ASP76 |
C | ILE77 |
C | THR158 |
C | ARG159 |
C | VAL160 |
C | GLY163 |
C | MET164 |
C | TRP168 |
C | THR169 |
C | CYS170 |
C | ALA171 |
C | VAL281 |
C | CYS283 |
C | THR319 |
C | ALA320 |
C | HIS324 |
C | LEU547 |
C | ASN593 |
C | PRO594 |
C | THR595 |
C | HOH911 |
C | HOH967 |
C | HOH986 |
C | HOH997 |
C | HOH1000 |
C | HOH1020 |
C | HOH1057 |
C | HOH1094 |
C | HOH1163 |
C | HOH1178 |
C | VAL52 |
C | GLY53 |
C | GLY55 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 12P C 802 |
Chain | Residue |
B | SER134 |
C | PRO144 |
C | ASP147 |
C | PRO148 |
C | HOH1204 |
C | HOH1213 |
C | HOH1233 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MES C 803 |
Chain | Residue |
C | GLY398 |
C | ALA399 |
C | SER400 |
C | ASN402 |
C | LYS403 |
C | HIS404 |
C | PRO405 |
site_id | AC9 |
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 | TRP168 |
D | THR169 |
D | CYS170 |
D | ALA171 |
D | VAL281 |
D | CYS283 |
D | THR319 |
D | ALA320 |
D | HIS324 |
D | LEU547 |
D | ASN593 |
D | PRO594 |
D | THR595 |
D | HOH935 |
D | HOH958 |
D | HOH1012 |
D | HOH1054 |
D | HOH1055 |
D | HOH1078 |
D | HOH1083 |
D | HOH1097 |
D | HOH1176 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 12P D 802 |
Chain | Residue |
A | SER134 |
D | PRO144 |
D | GLU145 |
D | GLN146 |
D | ASP147 |
D | PRO148 |
D | HOH1086 |
D | HOH1092 |
D | HOH1095 |