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 |