3WID
Structure of a glucose dehydrogenase T277F mutant in complex with NADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005536 | molecular_function | D-glucose binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019595 | biological_process | non-phosphorylated glucose catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
A | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
A | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
A | 0070401 | molecular_function | NADP+ binding |
A | 0070403 | molecular_function | NAD+ binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005536 | molecular_function | D-glucose binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019595 | biological_process | non-phosphorylated glucose catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
B | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
B | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
B | 0070401 | molecular_function | NADP+ binding |
B | 0070403 | molecular_function | NAD+ binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005536 | molecular_function | D-glucose binding |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019595 | biological_process | non-phosphorylated glucose catabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
C | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
C | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
C | 0070401 | molecular_function | NADP+ binding |
C | 0070403 | molecular_function | NAD+ binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0005536 | molecular_function | D-glucose binding |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019595 | biological_process | non-phosphorylated glucose catabolic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
D | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
D | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
D | 0070401 | molecular_function | NADP+ binding |
D | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1001 |
Chain | Residue |
A | CYS99 |
A | CYS102 |
A | CYS110 |
A | ASP116 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAP A 1002 |
Chain | Residue |
A | ASN216 |
A | ARG217 |
A | HIS218 |
A | TYR238 |
A | THR252 |
A | SER253 |
A | ASP255 |
A | THR258 |
A | PHE275 |
A | GLY276 |
A | PHE277 |
A | SER304 |
A | VAL305 |
A | ASP306 |
A | HOH1127 |
A | HOH1147 |
A | HOH1167 |
C | VAL295 |
A | ILE192 |
A | SER194 |
A | GLY195 |
A | SER196 |
A | GLU197 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGO A 1003 |
Chain | Residue |
A | ARG95 |
A | LEU125 |
A | HIS126 |
A | ARG130 |
A | TYR134 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1PE A 1004 |
Chain | Residue |
A | TYR82 |
A | ILE137 |
A | LEU140 |
A | VAL141 |
A | LYS142 |
A | LYS309 |
A | VAL313 |
B | ASP181 |
B | ILE185 |
B | GLY209 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 1PE B 4001 |
Chain | Residue |
A | ARG106 |
A | HOH1115 |
B | LYS173 |
B | GLN178 |
B | SER182 |
C | LYS173 |
C | ARG174 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 4002 |
Chain | Residue |
B | CYS99 |
B | CYS102 |
B | CYS110 |
B | ASP116 |
site_id | AC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAP B 4003 |
Chain | Residue |
B | ILE192 |
B | SER194 |
B | GLY195 |
B | SER196 |
B | GLU197 |
B | ASN216 |
B | ARG217 |
B | HIS218 |
B | TYR238 |
B | THR252 |
B | ASP255 |
B | THR258 |
B | PHE275 |
B | PHE277 |
B | SER304 |
B | VAL305 |
B | ASP306 |
B | HOH4125 |
B | HOH4129 |
B | HOH4197 |
D | VAL295 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGO B 4004 |
Chain | Residue |
B | ARG95 |
B | ALA120 |
B | HIS126 |
B | ARG130 |
B | TYR134 |
B | HOH4170 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE B 4005 |
Chain | Residue |
A | GLN178 |
A | SER182 |
B | ARG106 |
B | GLU166 |
B | HIS311 |
B | GLN314 |
B | HOH4119 |
B | HOH4200 |
D | ARG174 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 1PE B 4006 |
Chain | Residue |
B | ASP317 |
B | HOH4145 |
A | ASP181 |
A | ILE185 |
B | ILE137 |
B | LEU140 |
B | VAL141 |
B | LYS142 |
B | ASN144 |
B | LYS309 |
B | VAL313 |
B | LEU316 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 1001 |
Chain | Residue |
C | CYS99 |
C | CYS102 |
C | CYS110 |
C | ASP116 |
site_id | BC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAP C 1002 |
Chain | Residue |
A | VAL295 |
C | ILE192 |
C | GLY193 |
C | SER194 |
C | GLY195 |
C | SER196 |
C | GLU197 |
C | ASN216 |
C | ARG217 |
C | HIS218 |
C | TYR238 |
C | THR252 |
C | SER253 |
C | THR258 |
C | PHE275 |
C | PHE277 |
C | SER304 |
C | VAL305 |
C | ASP306 |
C | LYS349 |
C | HOH1129 |
C | HOH1131 |
C | HOH1147 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGO C 1003 |
Chain | Residue |
C | ARG95 |
C | HIS126 |
C | ARG130 |
C | TYR134 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1PE C 1004 |
Chain | Residue |
C | LEU140 |
C | VAL141 |
C | LYS142 |
C | ASN144 |
C | LYS309 |
C | VAL313 |
C | LEU316 |
C | ASP317 |
D | ASP181 |
D | ILE185 |
site_id | BC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1PE C 1005 |
Chain | Residue |
B | LYS173 |
B | ARG174 |
C | LYS173 |
C | ILE176 |
C | GLN178 |
C | ASN179 |
C | SER182 |
C | HOH1155 |
D | ILE104 |
D | ARG106 |
D | GLU166 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1PE D 4001 |
Chain | Residue |
A | LYS173 |
A | SER175 |
C | ILE104 |
C | ARG106 |
D | LYS173 |
D | ILE176 |
D | GLN178 |
D | ASN179 |
D | SER182 |
D | HOH4103 |
D | HOH4132 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 4002 |
Chain | Residue |
D | CYS99 |
D | CYS102 |
D | CYS110 |
D | ASP116 |
site_id | BC9 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAP D 4003 |
Chain | Residue |
B | VAL295 |
D | ASN160 |
D | ILE192 |
D | SER194 |
D | GLY195 |
D | SER196 |
D | GLU197 |
D | ASN216 |
D | ARG217 |
D | HIS218 |
D | TYR238 |
D | THR252 |
D | ASP255 |
D | THR258 |
D | PHE275 |
D | PHE277 |
D | SER304 |
D | VAL305 |
D | ASP306 |
D | HOH4114 |
D | HOH4158 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGO D 4004 |
Chain | Residue |
D | ARG95 |
D | HIS126 |
D | PHE128 |
D | ARG130 |
D | TYR134 |
D | ASP135 |
site_id | CC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 1PE D 4005 |
Chain | Residue |
C | ASP181 |
C | ILE185 |
D | ILE137 |
D | LEU140 |
D | VAL141 |
D | LYS142 |
D | ASN144 |
D | LYS309 |
D | VAL313 |
D | LEU316 |
D | ASP317 |
D | HOH4166 |